Camel Liver Research Articles

Exploring methandienone metabolites generated via homogenized camel liver: Advancements for anti-doping applications through High Resolution-Liquid Chromatography Mass Spectrometry analysis.

Anabolic steroids, also known as anabolic-androgenic steroids (AAS), encompass steroidal androgens such as testosterone, as well as synthetic counterparts with similar structures and effects. The misuse of AAS has increased over the years, leading to ethical and welfare concerns in sports. The World Anti-Doping Agency (WADA) and the International Federation for Equestrian Sports (FEI) have banned AAS in relevant sports. Methandienone is one of the most identified anabolic androgenic steroids in sports drug testing, Therefore, reliable detection methods are crucial for effective doping control and maintaining the integrity of the sports. This study explores the use of homogenized camel liver for detecting methandienone metabolites in camels. The biotransformation pathways of methandienone in homogenized camel liver tissues are analyzed using Liquid Chromatography-High Resolution Mass Spectrometry (LC-HRMS) to identify and characterize the phase I and phase II metabolites. Chromatographic separation was achieved using a Thermo-Hypersil C18 column. The study has identified 11 methandienone metabolites (M1-M11), this includes 10 phase I and one phase II metabolite. A glucuronic acid conjugate of methandienone was observed in this study, but no sulfonic acid conjugations were found. The metabolites and their possible chemical structures, along with their fragmentation patterns are confirmed using MSMS (MS2) experiments in data-independent acquisition (DIA) mode. These findings serve as a vital tool for the rapid detection of methandienone, combating its illicit use in camel racing. Comprehensive screenings covering both the parent drug and its metabolites are recommended to improve detection accuracy and ensure regulatory compliance in sports doping. Future research should explore methandienone's metabolite profile in administered camel samples.

Characterizing Lomerizine metabolites in camel urine: High‐resolution mass spectrometry method development and validation for enhanced doping control

RationaleLomerizine (LMZ) is an antimigraine drug that works as a calcium channel blocker and has selective effects on the central nervous system. It is metabolized into trimetazidine (TMZ), which is a prohibited substance owing to its performance‐enhancing effects in both human and animal sports. Effective doping control measures are imperative to distinguish the source of TMZ in samples to ensure integrity and fairness of the sport, therefore a comprehensive analysis of LMZ metabolites is essential to identify potential biomarkers in camel urine for effective doping control.MethodsCamel urine samples were collected from four healthy animals following a single oral administration of LMZ at a dosage of 1 mg/kg body weight. In vitro studies were conducted using homogenized camel liver samples. Lomerizine and its metabolites were extracted using solid‐phase extraction and analyzed with a Thermo Fisher Orbitrap Exploris liquid chromatography mass spectrometry system. The acquired data was processed with the Compound Discoverer software.ResultsThe study conducted a comprehensive analysis of LMZ metabolites in camels and identified 10 phase I and one phase II metabolites. The primary pathway for the formation of phase I metabolites was de‐alkylation, while phase II metabolite was formed through alkylation of the parent drug. The study provided valuable insights into the unique metabolic pathways of LMZ in camels under specific experimental conditions.ConclusionThe developed method enables the detection and characterization of LMZ and its metabolites in camels. The identified metabolites has the potential to act as marker metabolites for the distinctive detection of LMZ in camel urine to ensure efficient analytical strategies for routine doping control applications.

Effects of long-term dehydration on stress markers, blood parameters, and tissue morphology in the dromedary camel (Camelus dromedarius).

Dromedary camels robustly withstand dehydration, and the rough desert environment but the adaptation mechanisms are not well understood. One of these mechanisms is that the dromedary camel increases its body temperature to reduce the process of evaporative cooling during the hot weather. Stress in general, has deleterious effects in the body. In this study, we sought to determine the effects of dehydration and rehydration on stress parameters in the dromedary camels and how it pacifies these effects. Nineteen male camels were randomly divided into control, dehydrated and rehydrated groups, and fed alfalfa hay ad-libitum. The dehydrated and rehydrated groups were water-restricted for 20 days after which the rehydrated camels were provided with water for 72 h. The control and dehydrated camels were slaughtered at day 20 from the start of experiment whereas the rehydrated group was killed 72 h later. Many biochemical, hematological histopathological parameters and gene analysis were performed in relevant tissues collected including blood, plasma, and tissues. It was observed that severely dehydrated camels lost body weight, passed very hard feces, few drops of concentrated urine, and were slightly stressed as reflected behaviorally by loss of appetite. Physiologically, the stress of dehydration elicited modulation of plasma stress hormones for water preservation and energy supply. Our results showed significant increase in cortisol, norepinephrine and dopamine, and significant decrease in epinephrine and serotonin. The significant increase in malondialdehyde was accompanied with significant increase in antioxidants (glutathione, retinol, thiamin, tocopherol) to provide tissue protection from oxidative stress. The physiological blood changes observed during dehydration serve different purposes and were quickly restored to normality by rehydration. The dehydrated/rehydrated camels showed reduced hump size and serous atrophy of perirenal and epicardial fat. The latter changes were accompanied by significantly increased expression of genes encoding proteins for energy production (ANGPTL4, ACSBG1) from fat and significantly decreased expression of genes (THRSP; FADS 1&2) encoding proteins enhancing energy expenditure. This process is vital for camel survival in the desert. Dehydration induced no major effects in the vital organs. Only minor degenerative changes were observed in hepatic and renal cells, physiological cardiomyocyte hypertrophy in heart and follicular hyperplasia in splenic but lipidosis was not depicted in liver hepatocytes. Ketone bodies were not smelled in urine, sweat and breathing of dehydrated animals supporting the previous finding that the ß hydroxybutyrate dehydrogenase, a key enzyme in ketone body formation, is low in the camel liver and rumen. Rehydration restored most of blood and tissues to normal or near normal. In conclusion, camels are adapted to combat dehydration stress and anorexia by increasing anti-stressors and modulating genes involved in fat metabolism.

Investigation of in vitro generated metabolites of LGD-4033, a selective androgen receptor modulator, in homogenized camel liver for anti-doping applications.

The use of selective androgen receptor modulators (SARM) in sports is prohibited by the World Anti-Doping Agency (WADA) due to their potential as performance-enhancing drugs, offering an unfair advantage. LGD-4033 is a SARM known for its similarities to anabolic steroids and can be easily purchased online, leading to increased availability and misuse. Adverse analytical findings have revealed the presence of SARMs in dietary supplements. Although LGD-4033 misuse has been reported in human sports over the years, concerns also arise regarding its illicit use in animal sports, including camel racing. Although various studies have investigated the metabolism of LGD-4033 in humans, horse, and other species, there is limited research specifically dedicated to racing camels. This study focuses on the in vitro metabolism of LGD-4033 in homogenized camel liver using liquid chromatography-high-resolution mass spectrometry (LC-HRMS) to identify and characterize the metabolites. The findings indicated the presence of 12 phase I metabolites and 1 phase II metabolite. Hydroxylation was responsible for the formation of the main phase I metabolites that were identified. A glucuronic acid conjugate of the parent drug was observed in this study, but no sulfonic acid conjugate was found. The possible chemical structures of these metabolites, along with their fragmentation patterns, were identified using MS. These findings provide valuable insights into the metabolism of LGD-4033 in camels and aid in the development of effective doping control methods for the detection of SARMs in camel racing.

Comprehensive metabolite profiling of trimetazidine in camels using high-resolution accurate mass spectrometry: Implications for doping control.

Trimetazidine and its metabolites are prohibited substances in sports. With a growing number of adverse findings in human athletes, it is crucial to develop doping control strategies that include screening for trimetazidine in animal sports. This study aims to detect and characterize trimetazidine and its metabolites for doping control in camel racing. Camel urine and plasma samples were collected from four healthy animals following a single oral dose of trimetazidine. In vitro investigations were conducted using camel liver samples. Liquid-liquid extraction and solid-phase extraction techniques were employed for the extraction of trimetazidine metabolites from plasma and urine matrices. The metabolites were analyzed using a Thermo Orbitrap Exploris LC-MS system with optimized settings to achieve maximum sensitivity and accurate mass measurements. Comprehensive metabolite profiling of trimetazidine in camels revealed the identification of seven phase I and five phase II metabolites. Phase I metabolites were primarily formed through dealkylation, while phase II metabolites were dominated by glucuronide conjugation of demethylated trimetazidine. The findings provided insights into the distinct metabolic pathways and biotransformation patterns of trimetazidine in camels under the experimental conditions. The developed method enables detection and characterization of trimetazidine and its metabolites in camels. The identified metabolites have the potential to serve as marker metabolites for trimetazidine abuse in camel racing. This study provides valuable insights into the metabolism of trimetazidine in camels.

Identification of in vitro metabolites of boldenone using Camel liver microsomes – A HR-LCMS approach

Anabolic steroids are widely abused in animal sports to improve their performance. The present study identifies the possible metabolites of boldenone in camel liver. A high-resolution accurate QE mass spectrometer was used to identify the parent boldenone and its metabolites. To investigate the phase 1 biotransformation of boldenone in camel, sodium phosphate buffer and NADPH were used. Chromatographic separation was carried out on a Thermo Hypersil C18 column using acetonitrile and formic acid as mobile phases. The current study, helped in unequivocal detection of six metabolites (Phase 1) for boldenone. The 17b-boldenone is an 3-oxo-Delta (1), Delta(4)-steroid substituted by an oxo group at position 3 and a beta-hydroxy group at position 17. It is prone to oxidation, which results in three hydroxylated metabolites with protonated parent ion of m/z 303.1954 (C19H27O3)+. Androsta-1,4-diene-3,17-dione [M+H]+ of m/z 285.1848 (C19H25O2+), hydroxyandrosta-1,4-diene-3,17-dione [M+H]+ of m/z 301.1797 (C19H25O3+) in addition to 17-hydroxy-androsta-1-en-3-one [M+H]+ of m/z 289.2162 (C19H29O2+) were also identified. The structures of the detected metabolites were identified based on their accurate mass, fragmentation pattern, and chromatographic retention time. In this research, camel liver was successfully used for in vitro experiments as an alternative to liver microsomes.

Camel Proteins and Enzymes: A Growing Resource for Functional Evolution and Environmental Adaptation.

In less agroecological parts of the Asian, Arabian, and African deserts, Camelus dromedarius play an important role in human survival. For many years, camels have been employed as a source of food, a tool of transportation, and a means of defense. They are becoming increasingly important as viable livestock animals in many desert climates. With the help of camel genetics, genomics and proteomics known so far, this review article will summarize camel enzymes and proteins, which allow them to thrive under varied harsh environmental situations. An in-depth study of the dromedary genome revealed the existence of protein-coding and fast-developing genes that govern a variety of metabolic responses including lipid and protein metabolism, glucoamylase, flavin-containing monooxygenase and guanidinoacetate methyltransferase are other metabolic enzymes found in the small intestine, liver, pancreas, and spleen. In addition, we will discuss the handling of common medications by camel liver cytochrome p 450, which are different from human enzymes. Moreover, camels developed several paths to get optimum levels of trace elements like copper, zinc, selenium, etc., which have key importance in their body for normal regulation of metabolic events. Insulin tolerance, carbohydrate and energy metabolism, xenobiotics metabolizing enzymes, vimentin functions, behavior during the rutting season, resistance to starvation and changes in blood composition and resistance to water loss were among the attractive aspects of camel enzymes and proteins peculiarities in the camels. Resolving the enigma of the method of adaptation and the molecular processes linked with camel life is still a developing repository full of mysteries that need additional exploration.

Effect of organic additives on storage stability of camel liver catalase against environmental conditions

The storage stability of catalase is very low under practical reaction conditions. Therefore, this study is aimed to evaluate the storage stability of catalase from camel liver by treated it with polyethylene glycol (PEG), glycerol, bovine serum albumin (BSA) and glucose against different storage conditions. The effect of some additives as stabilizers on the storage stability of camel liver catalase at 4°C and 30°C after 30 and 90 days was studied. The enzyme with additives at 5%concentration was more stable at 4 and 30°C for 90 days of incubation than native enzyme. The activity of catalase was more thermal stable in presence of 5%additive. The activity of enzyme with 5%BSA and glucose was retained 60%of its activity at 60°C. At pH 11 the catalase with glucose retained 30%of its activity. The native enzyme lost 80%of its activity in presence of 5 mM β-mercaptoethanol, where the enzyme with additive retained 30–46%of its activity. At 8 M urea, the native enzyme and enzyme with 5%of all additives retained 28%and 61–77%of its activity, respectively. The catalase with additives retained 50–90%of its activity in presence of different dyes. The results appeared that the catalase with additives may be used for elimination of excess of hydrogen peroxide after bleaching of textile.

Heavy Metal Accumulation, Tissue Injury, Oxidative Stress, and Inflammation in Dromedary Camels Living near Petroleum Industry Sites in Saudi Arabia

Simple SummaryThe petroleum industry is a major source of energy and economic development but can pollute the environment and negatively impact animal and human health. Heavy metals are environmental pollutants and can reach the human body in direct and indirect ways. We investigated the levels of heavy metals in the soil and in the milk, blood, muscle, liver, and kidney of Arabian camels living near a petroleum industry site in the eastern region of Saudi Arabia. Our results revealed increased lead levels, cadmium, nickel, and vanadium in the soil and different tissues of camels. In addition, liver and kidney dysfunction, tissue damage, oxidative stress, inflammation, and apoptosis were reported. These findings may be of public interest and call attention to the assessment of the impact of the petroleum industry on the environment and the health of nearby communities.The petroleum industry can impact the environment and human health. Heavy metals (HMs), including lead (Pb), cadmium (Cd), nickel (Ni), and vanadium (V), are toxic pollutants found in petroleum that can cause several severe diseases. This study investigated the impact of the oil industry on the Arabian camel (Camelus dromedarius) in the eastern region of Saudi Arabia, pointing to HMs accumulation, tissue injury, redox imbalance, inflammation, and apoptosis. Soil and camel samples (milk, blood, muscle, liver, and kidney) were collected from a site near an oil industry field and another two sites to analyze HMs. Pb, Cd, Ni, and V were increased in the soil and in the camel’s milk, blood, muscle, liver, and kidney at the polluted site. Serum aminotransferases, urea, and creatinine were elevated, and histopathological alterations were observed in the liver and kidney of camels at the oil industry site. Hepatic and renal lipid peroxidation, pro-inflammatory cytokines, Bax, and caspase-3 were increased, whereas cellular antioxidants and Bcl-2 declined in camels at the oil extraction site. In conclusion, the oil industry caused soil and tissue accumulation of HMs, liver and kidney injury, oxidative stress, and apoptosis in camels living close to the oil extraction site. These findings pinpoint the negative impact of the oil industry on the environment, animal, and human health.

Scorpion crude venom induced apoptosis and structural changes of Echinococcus granulosus protoscolices

Echinococcus granulosus parasitic infection in humans causes hydatidosis (also known as echinococcosis), which is a severe zoonotic illness that puts public health at risk.This research was designed to assess the status of morphological, ultrastructure, and cell apoptosis of E. granulosus protoscolices. For this purpose, the protoscolices were isolated and collected from the hydatid cysts in the lungs and livers of camels, then incubated for 4 h in Androctonus crassicauda crude venom (ACCV) (at the concentrations of 50 and 100 µg/ml). The changes of E. granulosus protoscolices were monitored using light, transmission, and scanning electron microscopy, and the caspase-3 expression was detected by immunohistochemistry. The current study results have demonstrated the caspase-3 expression was substantially higher in the protoscolices incubated at 100 µg/ml than 50 µg/ml. Also, ACCV caused distinct changes in the morphology and ultrastructure of protoscolices detected by light, TEM, and SEM microscopy. In conclusion, Androctonus crassicauda crude venom (ACCV) may provide an alternative and nonsurgical treatment for hydatidosis. Hence, further studies are recommended to explore the impact of ACCV on inducing apoptosis and structural changes for this parasitic disease.

Occurrence of Aflatoxins in Livers and Milk of Camels in Saudi Arabia

The objective of the present study was to detect and quantify aflatoxins in liver and milk of camels. HPLC method was used to detect different aflatoxins. Liver samples were collected from slaughterhouses and milk samples from breeder's sites in Eastern Province, Saudi Arabia. Samples of camel livers and milk (250 samples of each) were collected and analyzed. About 26.4 and 16% of livers showed a contamination level in the range of 0.4-1 ng/g aflatoxin B1 and B2, respectively, but there were no detectable levels of G1, G2, M1 and M2. About 29.7% of milk samples had a range of aflatoxin M1 of 15-50 ng/l and 6% had a range of 50-100 ng/l. However, M2 was not detected in any milk sample. Based on regulatory limits, the present values of aflatoxin in livers and milk were within the internationally accepted limits (permissible limits of aflatoxins are 0.5 ppb for liver and liquid milk, according to the Saudi Organization for Standardization, Meteorology and Quality, (SASO).

Immobilization of Camel Liver Catalase on Nanosilver-Coated Cotton Fabric

Nanoparticles have the advantage of a superior surface area to volume ratio, and thus such materials are useful for enzyme immobilization. A silver nanoparticle coated cotton fabric (AgNp-CF) is used to immobilize camel liver catalase in the present work. The effect of loading levels of AgNp inside cotton fabrics on the immobilization of catalase was investigated. The results revealed that a 6 mL loading level of AgNp precursor (silver nitrate, 2 mM) at pH 8 showed the maximum immobilization efficiency (76%). The morphological properties of the cotton fabric (CF), AgNp-CF and AgNp-CF-catalase were characterized by SEM. The reusability of the immobilized enzyme was tested over ten reuses to show a 67% retained function of its initial activity. Compared with the soluble enzyme’s working pH (6.5), a rather broader working pH (6.5–7.0) was observed for the immobilized catalase. Additionally, the optimum working temperature increased from 30 for the soluble enzyme to 40 °C for the immobilized one, indicating thermal stability. The free and immobilized catalase enzyme’s Km values were 22.5 and 25 mM H2O2, respectively, reflecting the enzyme’s effective properties. The inhibitory effect of metal ions on the enzyme activity was higher toward soluble catalase than the immobilized catalase. This work has developed a method for immobilizing catalase to be useful for several applications.

Pathological and molecular investigations of systemic form of camelpox in naturally infected adult male dromedary camels in India

Camelpox is a wide-spread infectious viral disease of camelids. An outbreak of camelpox was reported in 15 adult male dromedary camels aged between 10 to 16 years of an organized herd in winter season. The infected camels showed clinical signs of fever, anorexia, lachrymation, pendulous lips, excessive salivation and pock lesions on the skin of head, neck, mouth, lips, extremities, thigh, abdomen, scrotum and inguinal region. Mortalities were recorded in three infected camels after 10–12 days of infection and showed systemic pox lesions characterized by vesicles, papules, ulcerations and raised pock lesions in the mucous membranes of the mouth, tongue, tracheal mucosa, lung, abomasum and liver. Histopathology study revealed characteristic pox lesions with intracytoplasmic eosinophilic inclusion bodies in tongue. Lung showed lesion of interstitial pneumonia (n = 2) and bronchointerstitial pneumonia (n = 1). Liver showed infiltration of mononuclear cells around central veins and degenerative changes of hepatocytes. The abomasum and intestine showed ulcerations, marked capillary congestion and areas of lymphocyte infiltration in mucosa and submucosa. The presence of camelpox virus (CMLV) was confirmed in viral DNA isolated from formalin fixed paraffin embedded (FFPE) tissues of tongue, lung, abomasum, liver, heart and intestine of infected camels by C18L gene PCR. The sequencing of viral DNAs showed phylogenetic relatedness with other CMLV isolates from India and other countries. Thus, our study confirmed the rare severe form of systemic camelpox outbreak in adult male dromedary camels hence future attention should be given for studies on virulence, strain identification and molecular epidemiology of CMLV for planning of effective preventive and control strategies.

Efficient sequestration of carbon dioxide into calcium carbonate using a novel carbonic anhydrase purified from liver of camel (Camelus dromedarius)

Abstract Carbonic anhydrase (CA) was successfully used for carbon dioxide (CO2) sequestration. In fact, sequestration of CO2 into value-added products, calcium carbonate (CaCO3), requires a stable and efficient CA that should tolerate high concentrations of CO2 and Ca2+, high pH and high temperature of working process. Herein, for the first time, the present manuscript described the sequestration of CO2 into CaCO3 using a novel CA which was purified and characterized from liver of camel (Camelus dromedarius), an animal that survive extreme desert conditions. The enzyme was a monomer with lower molecular weight (25 kDa), contained Fe as a physiologically-relevant cofactor instead of Zn and showed higher optimum pH (pH 9.0) and temperature (45°C). In addition, the enzyme was active and stable at strongly alkaline pH (pH 9.0) and higher temperature (60°C). IC50 values revealed that camel liver CA was inhibited by metal ions in the following order: Cu2+ > Zn2+ > Fe3+ > Cr3+ > Ni2+ > Cd2+ > Co2+ > Al3+ > Mg2+ > Ca2+, the enzyme needed high concentrations of Ca2+ to reach 50% inhibition. Camel liver CA was effective in accelerating CaCO3 formation in presence of 1, 2, 5, 10 and 20% Ca2+. The formed CaCO3 was characterized by SEM, XRD and FTIR. Interestingly, camel liver CA showed high CO2 sequestration capacity (966.67 mg CaCO3/mg enzyme) in presence of high concentration of Ca2+ (up to 20%). Camel CA represents promising candidate for harsh industrial applications.

Purification and characterization of l-glutaminase enzyme from camel liver: Enzymatic anticancer property

l-Glutaminase has gained an important attention as glutamine-depleting enzyme in treatment of various cancers. Therefore, this study aimed to purify, characterize and investigate antitumor activity of l-glutaminase from camel liver mitochondria (CL-Glu), since no available information about CL-Glu from camel. CL-Glu was purified using cell fractionation, ultrafiltration, DEAE-and CM-cellulose chromatography columns. The purified CL-Glu was a monomer with a molecular weight of 70 ± 3 kDa, isoelectric point of 7.2, optimum temperature of 70 °C and it was active over a broad pH range with a pH optimum at pH 8.0. Its activity had a clear dependence on phosphate ions. The studied enzyme showed sigmoidal kinetics, indicated its allosteric behavior with Km of 36 ± 4 mM and Hill coefficient of 1.5 which suggested a positive cooperatively of active sites. The purified l-glutaminase exerted antitumor activity against different cell lines with the highest cytotoxic activity against Hepatocellular carcinoma cell line (HepG-2) with an IC50 value of 152 µg/ml. In conclusion, l-glutaminase was purified from camel liver using simple methods and its unique properties such as stability at both wide pH range and at high temperature along with its relatively low molecular weight, facilitated its usage in medical applications as antitumor drug.

The Arabian camel, Camelus dromedarius interferon epsilon: Functional expression, in vitro refolding, purification and cytotoxicity on breast cancer cell lines.

The current study highlights, for the first time, cloning, overexpression and purification of the novel interferon epsilon (IFNƐ), from the Arabian camel Camelus dromedaries. The study then assesses the cytotoxicity of IFNε against two human breast cancer cell lines MDA-MB-231 and MCF-7. Full-length cDNA encoding interferon epsilon (IFNε) was isolated and cloned from the liver of the Arabian camel, C. dromedarius using reverse transcription-polymerase chain reaction. The sequence analysis of the camel IFNε cDNA showed a 582-bp open reading frame encoding a protein of 193 amino acids with an estimated molecular weight of 21.230 kDa. A BLAST search analysis revealed that the C. dromedarius IFNε shared high sequence identity with the IFN genes of other species, such as Camelus ferus, Vicugna pacos, and Homo sapiens. Expression of the camel IFNε cDNA in Escherichia coli gave a fusion protein band of 24.97 kDa after induction with either isopropyl β-D-1-thiogalactopyranoside or lactose for 5 h. Recombinant IFNε protein was overexpressed in the form of inclusion bodies that were easily solubilized and refolded using SDS and KCl. The solubilized inclusion bodies were purified to apparent homogeneity using nickel affinity chromatography. We examined the effect of IFNε on two breast cancer cell lines MDA-MB-231 and MCF-7. In both cell lines, IFNε inhibited cell survival in a dose dependent manner as observed by MTT assay, morphological changes and apoptosis assay. Caspase-3 expression level was found to be increased in MDA-MB-231 treated cells as compared to untreated cells.

Study of the circulatory energy balance indicators and hepatic fat content in dromedary camel during late pregnancy and early lactation

Lipid metabolism is a hallmark of energy metabolism in periparturient animals. Due to the lack of reports on fat metabolism during the transition period in camels, this study aimed to manifest the fluctuations in the fat metabolism indicators in serum and liver of camels during this period. Ten multiparous (with the parity of 2.38 ± 0.56; mean ± SEM) camels with a body weight of 527.94 ± 73.46 kg were studied 60 days antepartum (AP) until 60 days post-partum (PP). Blood was sampled at about (± three days) 60, 45, 30, 15, and three days before parturition, at parturition, and at the same time points during PP. Liver samples were collected through blind biopsy at about 15 days before calving, and at the same time points with blood collection during PP. No significant difference was observed for the concentration of TAG in the liver between days 15 AP until 3 PP. A definite increase was observed for liver TAG content at day 15 AP, which decreased gradually afterward (P < 0.05). Liver glycogen after an abrupt fall at parturition (P < 0.01), escalated during PP. Circulatory glucose decreased 15 days AP (P = 0.03) and did not return to the previous level until the end of the investigation. Right before parturition, serum TAG was distinctly low, but ascended 15 days PP (P < 0.05), and remained quite constant until the end of the study. Total lipid, phospholipids, HDL, and VLDL, were lowest at parturition (P < 0.05), then escalated temporally. As expected the correlation between serum concentrations of NEFA and β-hydroxybutyrate (BHB) during days 15 AP and 60 PP were highly positive (0.74; P < 0.01). Although hepatic TAG content was positively correlated with serum NEFA and BHB (P < 0.01), glycogen content of the liver revealed highly negative (P < 0.01) correlation with these two serum metabolites (both −0.75). This study, for the first time, denoted the preeminent fluctuations in lipid metabolism indicators during the physiological transition in pregnant camels. These results may be useful for comparative studies between camels and other species.

HISTOPATHOLOGICAL AND ULTRASTRUCTURE FEATURES OF HYDATID CYST FROM SLAUGHTERED ANIMALS IN EGYPT

In the current study, the hydatid cyst-induced tissue lesions in liver and lung of camels and sheep infected with Egyptian strain of E. granulosus was evaluated and the fine structures of the protoscolices by scanning electron microscope (SEM) was described. The results indicated that both fertile and sterile hydatid cysts could lead to various degree of tissue lesions visualized mainly as necrosis, inflammatory cell infiltration and tissue degeneration other histopathological changes occurred in lung and liver of infected animals due to infection with hydatid cyst. Tissue lesion associated with hydatidosis was described. SEM showed envaginated, invaginated protoscolex and the broad capsule of hydatid cyst. There were two types of hooks, large (upper row) and small (lower row) in hydatid cyst protoscolices; with microtriches on different regions.

Reporting temporal fluctuations of hepatic C16 and C18 fatty acids during late gestation and early lactation in dromedary camel.

Based on current knowledge, C16 and C18 fatty acids (FA) are considered the most functional FA in hepatic metabolism. Although these FAs have been satisfyingly investigated in cattle, other species such as camel have been neglected. For this reason, the current study was designed to scrutinize changing patterns of C16 and C18 FAs in 10 dromedary camels from the last 2months of gestation to the firstmonths of lactation. Camels were grazed on natural pasture and supplemented with a balanced ration. Liver biopsies were obtained through blind biopsy technique at about 60, 45, 30, and 15-day antepartum (AP), and at 3, 15, 30, 45, and 60 post-partum (PP). Data were analyzed by the ANOVA procedure of SPSS with repeated measurements. From 15-day AP, saturated FA content of the liver declined (P < 0.01) and 15-day PP reached its peak (P = 0.02). At 30-day PP it went down (P < 0.01), and re-elevated at 45-day PP (P < 0.01) but remained at a steady state for the duration of the study. Mono-unsaturated and polyunsaturated FA content of hepatic tissue were constant throughout AP, albeit observed to peak at 15-day AP compared with 45 (P = 0.04) and 30-day AP (P < 0.01) for mono-unsaturated FAs, and with 60-, 45-, and 30-day AP (P ≤ 0.01) for polyunsaturated FAs. The palmitic acid content of the liver reached a nadir at 30-day AP (P < 0.01), increased sharply (P < 0.01) at the next sampling time-point, and had a trend to escalate until 3-day PP. Palmitoleic acid levels were unchanged from 60- to 30-day AP, decreased at 15 AP and 3-day PP, increased at 15-day PP, then remained constant until the end of the study period (P ≤ 0.04). Stearic acid content started to grow at 15-day AP and reached its peak at 15-day PP (P < 0.01). At 30-day PP, stearic level in liver dropped abruptly (P < 0.01), then intensified at 45-day PP and did not change after; hepatic content of stearic acid was lower during AP compared with PP time-points. Other C18 FAs changed significantly during the study period. These results suggest that parturition could have a profound effect on FA composition and other metabolites in camel liver. Further research is required to establish the metabolic mechanism behind these changes.

Purification and biochemical characterization of a novel copper, zinc superoxide dismutase from liver of camel (Camelus dromedarius): An antioxidant enzyme with unique properties

A novel copper, zinc superoxide dismutase (CuZnSOD) was purified to homogeneity from the liver of an animal well adapted to the stressful living conditions of the desert, the camel (Camelus dromedarius). The biochemical properties of camel liver CuZnSOD were examined. The purified enzyme had a native molecular weight of 28 kDa, as judged by gel filtration chromatography, and showed a single band at 27 kDa on SDS-PAGE, indicating that it is a monomeric protein. Optimal activity of the purified enzyme occurred at 43 °C and pH 6.0, and the activation energy was 1.42 kJ/mol. CuZnSOD activity was strongly inhibited by β-ME, DTT, H2O2 and SDS and slightly inhibited by EDTA, NaN3 and PMSF. Al3+, Ca2+, Cd2+, Mg2+ and Zn2+ stimulated CuZnSOD activity, whereas Ba2+, Co2+, Fe2+ and Ni2+ inhibited it. The purified enzyme contained 0.010 µg of Cu and 0.69 µg of Zn per mg of protein. Km, Vmax, kcat and kcat/Km values for NBT and riboflavin were 16.27 and 0.16 µM, 20.85 and 21.54 U/mg, 9.65 and 9.97 s−1, and 0.59 and 62.33 s-1 µM−1, respectively. Camel liver CuZnSOD exhibited unique biochemical properties compared to those of other CuZnSODs, including lower molecular weight with a monomeric structure, higher optimum temperature, very low Ea, very low optimum pH, very low contents of Cu and Zn, and higher affinity, turnover number and catalytic efficiency for riboflavin. These unique properties of camel liver CuZnSOD might be related to the ability of this animal to inhabit stressful desert conditions.