Chicken Extract Research Articles

Antihypertensive effects of chicken extract against deoxycorticosterone acetate-salt-induced hypertension in rats.

We investigated the antihypertensive effect of Brand's Essence of Chicken (BEC), a popular chicken extract used as a traditional remedy, using deoxycorticosterone acetate (DOCA)-salt hypertensive rats. Animals were unilaterally nephrectomized, and then separated into a sham-operated group (sham group) and a DOCA-salt-treated group. The latter was further separated into a normal diet group and a BEC (freeze-dried powder, 0.1 w/w%)-containing diet group. Systolic blood pressure of the normal diet group progressively increased in comparison with that of the sham group. The DOCA-salt-induced hypertension was markedly suppressed by feeding a BEC-containing diet. Systolic blood pressure after 5 weeks was 128+/-2 mmHg in sham group, 181+/-4 mmHg in the DOCA-salt-treated normal diet group and 139+/-5 mmHg in the DOCA-salt-treated BEC diet group, respectively. The treatment with DOCA and salt for 5 weeks significantly increased the weights of heart and left ventricle, but these increases were significantly suppressed in the BEC group. When the degree of vascular hypertrophy of the aorta was histochemically evaluated, DOCA-salt-induced increases in wall thickness and wall area of the vessels were significantly decreased by the BEC-feeding. Histopathological renal damage of fibrinoid-like necrosis in glomeruli, thickening of small arteries and tubular dilatation were observed in the DOCA-salt-treated normal diet group, but this damage was efficiently reduced by the BEC-feeding. In addition, BEC-feeding decreased urinary excretion of protein, which was elevated by the treatment with DOCA and salt. Thus, BEC seems to be useful as a prophylactic treatment in the development of hypertension and related tissue injuries.

Meat allergy: investigation of potential allergenic proteins in beef.

The potential allergenic proteins in beef were investigated. The sera of ten beef-allergic patients suffering from atopic dermatitis and having a positive RAST score to beef, aged 3-18 years, were obtained from Yoshida Hospital in Japan, and five non-allergic individuals were subjected to this study. The sera of the ten patients reacted strongly to a beef extract, but not to pork and chicken extracts by both ELISA and immunoblotting. The sera of the five control subjects did not react to any of these meat extracts. Three bands having molecular masses of approximately 200 kDa, approximately 67 kDa and approximately 60 kDa were observed by immunoblotting after SDS-PAGE. Two fractions of the beef extract from a Sephadex-gel (G-200) filtration column strongly reacted with the sera of the beef-allergic patients by ELISA and immunoblotting: one fraction had the approximately 67 kDa component and the other had the approximately 200 kDa and approximately 60 kDa components. One of them (approximately 67 kDa) was confirmed to be bovine serum albumin (BSA) by an analysis of the N-terminal amino acid sequence. We could not identify the others by sequencing, but the approximately 200 kDa and approximately 60 kDa components were presumed to be glycoproteins. Bovine gamma (BGG:globulin M.W. approximately 160 kDa) is a glycoprotein and has several subunits. The beef-allergic patients showed strong reactivity to the approximately 200 kDa and approximately 60 kDa components of pure BGG by immunoblotting. Inhibition-ELISA showed that pure BGG preparations strongly inhibited the binding of sera from the beef-allergic patients to the beef extract. These results suggest that the approximately 200 kDa, approximately 67 kDa and approximately 60 kDa components in the beef extract had strong allergenicity: approximately 67 kDa was BSA, and approximately 200 kDa and approximately 60 kDa were presumably aggregated BGG and it's heavy chain, respectively.

Common allergens in avian meats

Background: Reports of allergy to bird meats are uncommon, and most have been in patients with “bird-egg syndrome.” Objective: We sought to evaluate 3 patients who reported allergic reactions to several avian meats, but who denied allergic reactions to eating eggs. The patients required yellow fever vaccine for entry into the military. Methods: Patients were skin tested with commercial extracts of chicken, turkey, and egg, as well as with crude extracts made from dove and quail meat, and with yellow fever vaccine. Immunoblots for IgE antibody were performed by using the same materials used for skin testing plus extracts of duck and goose meat. Results: Skin tests were positive in all 3 patients to chicken, turkey, dove, quail, and yellow fever vaccine and negative to egg. This included some positive skin test responses to bird meats the patients denied ever having eaten. The vaccine was administered in graded doses. Immunoblots revealed IgE binding to several proteins of similar molecular weights in all of the avian meats but not to egg or yellow fever vaccine. Again, this included IgE antibody to some bird meats the patients denied ever having eaten. Conclusion: Patients allergic to one bird meat may be allergic to others, including game birds, probably because of cross-reacting allergens. Such patients may have to exercise caution even when eating bird meats they have not previously ingested. The relationship of this allergy to yellow fever vaccine, if any, remains to be determined. (J Allergy Clin Immunol 1999;104:202-4).

Identification and localization of deoxyribonuclease I in the rat ovary.

Our objective was to identify the endonuclease responsible for DNA degradation in the ovary and determine its localization relative to the developmental state of ovarian follicles. Immature rats were treated with diethylstilbestrol (DES; DES group), DES + eCG (eCG group) or DES + eCG + hCG (hCG group). Nuclei of the eCG and hCG but not the DES group contained a 32/34-kDA DNase I-like endonuclease activity that was Ca2+/Mg(2+)-dependent, stimulated by Mn2+, optimal at pH 7, and identified by anti-DNase I antibody. G-actin, Zn2+, dithiothreitol, aurintricarboxylic acid, and sodium aurothiomalate, but not iodoacetic acid, inhibited the activity. Addition of eCG nuclear protein extracts to nuclei from the DES group induced oligonucleosomal DNA fragmentation, which could be prevented by pretreatment of the extracts with anti-DNase I antibody. DNase I was immunolocalized in nuclei of healthy luteal cells, antral follicle granulosa cells, oocytes of preantral follicles, atretic preantral follicles, and testicular spermatogonia, but was not observed in granulosa cells of preantral follicles, theca cells, antral follicle oocytes, or testicular spermatocytes. Nuclear extracts of rat kidney, liver, and spleen, and bovine, chicken, and human ovaries displayed DNase I-like activity. These results suggest that an endonuclease indistinguishable from DNase I is responsible for ovarian apoptotic DNA degradation.

Biochemical Characterization of Mouse Liver IBE1-Amide Immunoreactivity: Limitations of Antibody-Based Approaches for Verification of Peptide Expression

A high titer, specific antiserum, raised against a synthetic analogue of a unique peptide region within the human IGF-IB prohormone, detected specific immunoreactivity in extracts of mouse, chicken, sheep, and human liver. Specificity was confirmed by the ablation of immunoreactivity in the presence of excess synthetic immunogen. Here we report the isolation and characterization of one of the immunoreactive species from an extract of mouse liver: amino acid sequencing revealed that the purified product was 78% identical to the NH2-terminus of the α-subunit of mouse hemoglobin. Immunoblot analysis of a commercial preparation of mouse hemoglobin confirmed that the antiserum recognized hemoblobin. Addition of excess synthetic peptide to the antiserum eliminated the immunobinding to hemoglobin. The apparent “specificity” of even affinity-purified antiserum for hemoglobin provides a cautionary note for the interpretation of studies concluding antigen expression based solely on the presence of positive immunoreactivity.

Biochemical characterization of mouse liver IBE1-amide immunoreactivity: limitations of antibody-based approaches for verification of peptide expression.

A high titer, specific antiserum, raised against a synthetic analogue of a unique peptide region within the human IGF-IB prohormone, detected specific immunoreactivity in extracts of mouse, chicken, sheep, and human liver. Specificity was confirmed by the ablation of immunoreactivity in the presence of excess synthetic immunogen. Here we report the isolation and characterization of one of the immunoreactive species from an extract of mouse liver: amino acid sequencing revealed that the purified product was 78% identical to the NH2-terminus of the alpha-subunit of mouse hemoglobin. Immunoblot analysis of a commercial preparation of mouse hemoglobin confirmed that the antiserum recognized hemoglobin. Addition of excess synthetic peptide to the antiserum eliminated the immunobinding to hemoglobin. The apparent "specificity" of even affinity-purified antiserum for hemoglobin provides a cautionary note for the interpretation of studies concluding antigen expression based solely on the presence of positive immunoreactivity.

Confirmation of danofloxacin residues in chicken and cattle liver by microbore high-performance liquid chromatography electrospray ionization tandem mass spectrometry.

A specific assay is described for the confirmatory identification of danofloxacin residues in edible tissues of cattle and chicken. The assay utilizes on-line microbore high-performance liquid chromatography and pneumatically assisted electrospray tandem mass spectrometry (MS/MS). Collision-induced dissociation of the danofloxacin protonated molecule results in two significant daughter ions. Monitoring both ions provides the specificity required for this confirmatory assay. Optimum electrospray and MS/MS operating conditions permitted the specific monitoring of danofloxacin and the confirmation of its residues in chicken and cattle liver extracts down to 50 ppb. The analysis of control liver or the commercially available antibacterial quinolones enrofloxacin and its metabolite ciprofloxacin gave no response under the assay conditions. The ratios of the two daughter ions were similar for danofloxacin standard solutions, fortified tissues and incurred tissues.

Loss of poly(ADP-ribose) synthetase activity without change in arginine-specific ADP-ribosyltransferase activity by acid-treatment; application of the treatment to simple assay for transferase in the presence of poly(ADP-ribose) synthetase

We investigated the effects of acid treatment (pH 3.5) on the activities of arginine-specific ADP-ribosyltransferase (mono(ADPribosyl)transferase) (EC 2.4.2.31) and poly(ADP-ribose) synthetase (EC 2.4.2.30) purified from chicken liver, and we observed that the former enzyme retained completely its activity while there was no evidence for activity of the latter enzyme. Kinetic parameters, including K m values for NAD and whole histones in the reaction catalyzed by acid-treated ADP-ribosyltransferase, were the same as those in the reaction catalyzed by non-treated enzyme. The stereospecificities of the reaction forming ADP-ribosylarginine by acid-treated and non-treated ADP-ribosyltransferases were indistinguishable. We made use of this acid treatment to determine ADP-ribosyltransferase activity in chicken and chick-embryo liver extracts, with a filter assay. The enzyme activities (means± S.D. for three separate experiments) of 1-year-old chicken and 13-day-old chick embryo livers were 372.7 ± 80.20 and 110.6 ± 27.22 nmol ADP-ribose/g wet liver per h, respectively. This acid treatment is useful for f'fiter assay with labelled NAD of arginine-specific ADP-ribosyltransferase in the fraction containing poly(ADP-ribose) synthetase.

Brush border and cell adhesion of insect enterocytes have basic similarities with those of vertebrates

The molecular architecture of the brush border (BB) cytoskeleton of the vertebrate intestinal cells results to be well defined in its components. From the comparison of the protein profiles of chicken and larval BB extracts of Manduca sexta (Insecta, Lepidoptera) it emerges that cytoskeletal major components are the same and they have a similar localization in immunolabeled tissues. The smooth septate junctions (SSJs) of the midgut cells are localized in the most apical regions, where vertebrate intestinal cells exhibit the zonula occludens. We demonstrate that α-actinin, vinculin and myosin II are involved in the actin filaments-SSJ interaction. The insertion of microfilament bundles into submembranous F-actin/α-actinin/ vinculin complexes, discovered and described almost exclusively in vertebrate junctions of adherens type, results to be a more general system including the insect SSJs, that we have analyzed.

Identification and partial purification of a large, variant form of type XII collagen.

A large, alternate form of type XII collagen has been identified in cultures of the human epidermoid cell line WISH. This form, designated XIIA, is comprised of alpha chains that are approximately 90 kDa larger than the 220-kDa alpha chain previously characterized in extracts of fetal chicken and bovine tissues. Results from both collagenase digestion and rotary shadow analysis of partially purified material show that the increase is due to a larger NC3 domain. While both the large (XIIA) and the small (XIIB) forms of type XII collagen are identified in pulse-chase radiolabeling of fetal bovine skin explant culture, they are not related in a precursor-product fashion. Inhibition studies with alpha, alpha'-dipyridyl indicate that proper folding of the collagen helix is required for complete assembly and secretion of type XIIA in WISH cell culture. The 310-kDa alpha 1A chain is likely to represent the bovine equivalent of a second translation product, estimated to be 340 kDa, predicted from analysis of one complete chick cDNA sequence. Additionally, the amino-terminal amino acid sequence of the 220-kDa bovine alpha 1B chain was determined. This sequence is very near a potential alternate splice site predicted from analysis of chicken type XII cDNA.

Solubilization of the receptors for avian pancreatic polypeptide in chicken, canine, and pig brains.

When n-octyl-beta-D-glucoside was used in several detergents to extract active avian pancreatic polypeptide (APP) receptors, a specific binding of [125I]APP to the solubilized chicken cerebellar and porcine hippocampal membranes was found. The binding of [125I]APP to the solubilized receptors was dependent on incubation time, temperature, and protein concentrations and appeared to have a slightly acidic optimal pH. APP binding to chicken and porcine brain extracts showed a high specificity for APP, although the chicken receptors do not discriminate well between APP and its related peptides, neuropeptide Y and peptide YY. Scatchard analyses of competitive binding data indicated the presence of two classes of binding sites in the brain extracts as in membrane-bound receptors; however, the high affinity component of the chicken receptor showed a decreased affinity after extraction. APP receptors in chicken and porcine brain extracts retained their insensitivity to the nonhydrolyzable GTP analog guanosine 5'-O-(3-thiotriphosphate). Cross-linking studies were performed with the homobifunctional cross-linker disuccinimidyl suberate and brain membrane receptors solubilized with n-octyl-beta-D-glucoside. An APP receptor species with a M(r) of 67,000, the same size as that of the labeled protein in native membrane homogenates of chicken and pig brains, was identified. However, in the canine brain we observed a M(r) 85,000 receptor protein, suggesting that species differences exist among the structures of brain APP receptors. The solubilized cross-linked APP receptors in these species were adsorbed by wheat germ agglutinin-agarose and by concanavalin A, indicating that they are glycoprotein in nature. The availability of the solubilized receptors from vertebrate brains with n-octyl-beta-D-glucoside represents an important step toward the purification and molecular characterization of the APP receptors.

Fluorometric Determination of Thiamine Vitamers in Chicken

Abstract A comparison was made of the direct determination of thiamine In acidified heated chicken extracts, by either flow injection or chromatographic determination, with the standard method (acid and enzyme digestion, adsorption, and elutlon, followed by the fluorometric determination of thiochrome extracted by Isobutanol from K3Fe(CN)6-treated eluates). Liquid chromatography of extracts, followed by oxidation of thiamine vitamers to thlochromes, showed 1 light scatter emission peak and 2 thlochromes, the latter corresponding to thiamine and thiamine monophosphate. Both forms were determined quantitatively by flow Injection determination, the lower detection limit of which was about 60 femtomol. The determination was linear from 0.1 ng to 10 μg thlamlne/mL, and the pooled coefficient of variation was 4%. The determination of thiamine in chicken extracts provides a nondestructive method for determining thiamine and Its phosphate esters, either In toto by flow Injection determination or as individual components by chromatography.

Distribution and classification of acylphosphatase isozymes

Distributions of acylphosphatase isozymes among organs of several animal species were investigated. Organ extracts of pig and chicken were treated with isozyme-specific antibodies, subjected to electrophoresis on a polyacrylamide gel, then the gel was stained for acylphosphatase activity. Both animals showed three activity bands; one band was named common type isozyme because of its wide distribution in testis, muscle, brain, heart, spleen, kidney, liver, and erythrocyte, and the other two bands were named muscle type isozymes because of their localization in skeletal muscle. This classification was supported by selective and quantitative reactions of the isozymes to the isozyme-specific antibodies. Because the two bands of the muscle type have the same amino acid sequence and differ only in modifications on an SH group, it is suggested that pig and chicken have only the two major types of acylphosphatase. This conclusion was supported by similar experiments on dog, human, rabbit, and pigeon.

Biliary bile acid profiles of domestic fowl as determined by high performance liquid chromatography and fast atom bombardment mass spectrometry

1. 1. The biliary bile acid profiles of domestic chickens ( Gallus domesticus), turkeys ( Meleagris gallopavo), and ducks ( Anas platyrhynchos) were determiend by high performance liquid chromatography (HPLC) and fast atom bombardment mass spectrometry (FAB-MS). 2. 2. Chenodeoxycholyltaurine and cholyltaurine were the predominant bile acids in chicken and turkey bile, whereas duck bile contained primarily chenodeoxycholyltaurine and phocaecholyltaurine. 3. 3. Allocholyltaurine was also detected in chicken and turkey bile, but not in duck bile. 4. 4. FAB-MS analyses of individual HPLC peak fractions from chicken and duck bile extracts confirmed the presence of either taurine-conjugated dihydroxy- or trihydroxycholanoates. 5. 5. Direct FAB-MS analyses of avian bile extracts not subjected to HPLC permitted a rapid assessment of the relative proportion of taurine-conjugated dihydroxy- to trihydroxycholanoates.

Phylogenetic study on the immunoreactive atrial natriuretic peptide in the heart

Using two antisera against atriopeptin III (AP III) which had different characteristics in cross-reactivities with atrial natriuretic peptide (ANP) analogs, we have measured an immunoreactive ANP (ir-ANP) in the heart extracts of several species. ir-ANP in atrial extracts showed both high and low molecular weights. Serial dilutions of atrial extracts from chickens, turtles, frogs, and fish yielded competition curves which were parallel to the standard curve of AP III with antiserum No. 4. In comparison with two serial dilution curves of atrial extracts made using two antisera, No. 4 and No. 9, we suggest that the amino acid at position 12 of ir-ANP in the atrial extracts of chicken, turtle, frog, and fish is not isoleucine but is some other amino acid.

Development of an avian calcitonin radioimmunoassay using synthetic chicken calcitonin as immunogen

1. 1. A sequential double antibody radioimmunoassay (RIA) has been developed using synthetic chicken calcitonin (CT) as antigen, tracer and standard. 2. 2. The immunoassay has a minimum detection limit of 0.5 ng and effective dose ( ed 50 ) of 7 ng Serial dilutions of chicken and turkey plasma were parallel to serial dilutions of CT standard. Extracts of chicken and turkey ultimobranchial glands caused parallel displacement of tracer similar to synthetic CT. fli]3. Primary antisera (anti-chicken CT) was raised in guinea pigs immunized with RIBI; animals treated with Freund's complete adjuvant failed to respond. 3. 4. Chicken CT was determined to have a half-life of 60 sec in the turkey hen. Development of a homologous RIA for avian CT will allow studies to elucidate the role of this hormone in birds.

P‐epitope is characteristic for the neural tissue of vertebrates

In a search for antigens immunologically related to chordin, a notochord-specific glycoprotein of sturgeneous fishes, extracts from 55 samples of human and rabbit tissues were tested for inhibition of [125I]chordin binding to rabbit polyclonal antibodies. The strongest inhibition was observed with brain extracts of both species. Human, chicken, rabbit, and newt brain extracts also inhibited chordin binding in liquid phase to monoclonal antibodies (MAbs) against the P-epitope, the most immunogenic epitope of this glycoprotein. Immunohistochemical studies done on human and chicken embryos, newt, sterlet, and sturgeon embryos, larvae, and juveniles revealed a strong immunoreactivity of the brain, spinal cord, and tissue of the peripheral nervous system with an anti-P MAb. Other tissues, with several exceptions, showed a negative reaction in immunohistochemical experiments. The authors found that the P-epitope is ontogenetically expressed in the neural tissue of chicken, newt, and sterlet at the period of cytodifferentiation. Gel chromatography of human, chicken, and newt brain extracts showed that in each case the P-epitope was associated with a polydisperse macromolecular material of similar size. These antigens were designated as neurochordins. Prolonged pronase digestion of human and chicken brain extracts resulted in fragments with M about 3 kDa (presumably glycopeptides), which reacted with anti-P MAbs. These fragments were of the same size as corresponding glycopeptides of the pronase digest of chordin. Thus, in the present study, the P-epitope has been shown to be characteristic for the neural tissue of several vertebrate species; in the brain, it has been found in association with neurochordins, macromolecular antigens that are presumably protein conjugates with carbohydrates.

Sandwich ELISA for Detection of Pig Meat in Raw Beef Using Antisera to Muscle Soluble Proteins

A double-antibody sandwich ELISA (enzyme-linked immunosorbent assay) has been successfully developed for the detection of defined amounts of pig meat (1–50%) in raw beef. Antibodies against pig sarcoplasmic extracts were produced in rabbits. Pig-specific antibodies were affinity purified by removing antibodies which crossreacted with horse, chicken or beef extracts followed by immunoadsorption and elution from a pig-extract column. The ELISA involved capturing antigens in sarcoplasmic extracts with pig specific antibodies immobilized on 96-well plates, detecting bound antigen with pig specific, horseradish peroxidase-labeling antibody, and measuring peroxidase activity by the conversion of a clear substrate to a colored product.

Comparison of Four Methods for the Dimethylacetal‐free Formation of Fatty Acid Methyl Esters from Phospholipids of Animal Origin

ABSTRACTFatty acid methyl esters (FAMES) were prepared from phospholipid extracts of beef, pork, lamb, chicken and turkey using four methylating procedures: BF3/methanol, KOH/BF3, direct transesterification with KOH, and a commercial preparation, Meth Prep II. Gas chromatographic analysis of the FAMES revealed the presence of dimethyl acetals (DMAs) in samples methylated with BF3/methanol or KOH/ BF3. These DMAs were evident when samples were analyzed on both polar and non‐polar columns. DMAs were not found in samples derivatized by direct alkali transesterification or by Meth Prep II.

A potent hypotensive factor in chicken left ventricle.

Chicken artria and ventricles both have membrane-bound granules which resemble those containing atriopeptin (ANP) in mammals. However, nothing is known about the contents of the avian granules. A previous study in chickens showed that although extracts of whole chicken heart or synthetic rat ANP both caused profound hypotension, ANP caused both natriuresis and diuresis, while chicken heart extract did not. The present study sought to locate the region(s) of chicken heart containing the hypotensive activity, and to observe the effect on sodium and water excretion and blood pressure in rats. Acid extracts of either atrium, either ventricle, ventricular septum, skeletal muscle, and liver were identically prepared from chickens and rats. Extracts were adjusted to the same protein concentration and injected (0.15 ml/kg) into anesthetized Single Comb White Leghorn roosters. Mean arterial pressure (MAP) and the time for recovery were measured. The most potent extract from chicken hearts was from the left ventricle (-38 +/- 1 mm Hg, 149 +/- 9 sec to recover). All other extracts (including right ventricle) produced only small (10-20 mm Hg), short-lived (20-30 sec) decreases in MAP. In contrast, only rat atrial extracts evoked long-lasting hypotension (greater than 40 mm Hg, recovery time greater than 200 sec). A 30-min infusion of the most potent chicken extract (left ventricle, CLV) into rats produced a small but significant natriuresis and diuresis compared to the vehicle time control (P less than 0.05) and the hypotensive response to bolus injection was about one-third that seen in the chicken. The location of potent spasmolytic activity primarily in chicken left ventricle, the different avian renal responses to chicken heart extract and synthetic rat ANP (5), and the weak diuretic, natriuretic, and hypotensive effects of CLV extract in rats all suggest that the chicken heart substance may be different from mammalian ANP.