Beef Spleen Research Articles

Empal gentong and empal asem with packaged cans: traditional foods from Cirebon

There has been research on traditional cuisine from Cirebon, empal gentong and empal asem. This empal is one of a variety of Soto cuisine which uses a mixture of beef, tripe, beef spleen and cow innards. The method used was to compare the results of heat adequacy measurement at 121°C for 60 minutes (starting from pushing ON button of the equipment), then the canned product can be analysed, both physical and nutritional value between 2 different variant types of empal gentong and empal asem. The result of the research obtained by empal Gentong Heat adequacy is 21.24 minutes with a net weight of 24.4%, aw 0.882, pH 5.93, water content of 83.9%, Ash 1.53%, 7.82% protein, fat 3.07%, carbohydrate 3.68%, sugar 2.39% with total energy of 220 calories. While the result of heat adequacy empal asem is 20.36 minutes with a net weight of 25.9%, aw 0.884, pH 5.42, water content 86.5%, Ash 1.66%, protein 6.89%, fat 0.84, carbohydrate 4.11%, sugar 2.21% with a total energy of 150 calories. Based on Regulation of the Head of the Food and Drug Supervisory Agency - Republic of Indonesia (BPOM RI) Number 24 of the year 2016 concerning Commercial Sterile Food Requirements, Chapter III Requirements for Sterile Commercial Foods Article 3, paragraph 2 that sterility value (F0) is at least 3.0 minutes calculated against Clostridium botulinum spores. Thus, canned empal gentong and empal asem can be declared safe for consumption by consumers.

Prevalence and quantification of Listeria monocytogenes in beef offal at retail level in Selangor, Malaysia

A total of 63 beef offal samples (beef liver = 16; beef lung = 14; beef intestine = 9; beef tripe = 15; beef spleen = 9) from three wet markets (A, B, and C) in Selangor, Malaysia were examined for the prevalence and microbial load of Listeria monocytogenes. A combination of the most probable number and polymerase chain reaction (MPN-PCR) method was employed in this study. It was found that L. monocytogenes detected in 33.33% of the beef offal samples. The prevalence of L. monocytogenes in beef offal purchased from wet markets A, B, and C were 22.73%, 37.50% and 41.18% respectively. The density of L. monocytogenes in all the samples ranged from < 3 up to > 2,400 MPN/g. The findings in this study indicate that beef offal can be a potential vehicle of foodborne listeriosis.

쇠고기 부산물로부터 혈압 상승 억제 펩타이드 분리 및 정제

ABSTRACT Angiotensin-
Iconverting enzyme(ACE)inhibitor was isolated from beef by-products. The beef by- product hydrolysates prepared with various proteases were tested for the inhibitory effects against ACE. The proteases used were proteinase A from bakers yeast, protease type
O
I
fungal and thermolysin. The maximum inhibitory effect was observed after hydrolysis for 12hrs(beef heart) and 24hrs(beef spleen), respectively. After gel filtration, IC 50 value was 0.37mg/L
in beef heart and 1.84mg/L
in beef spleen. After RP-HPLC, the IC 50 value of peak 1, peak 2, peak 3 and peak-4 were 0.28mg/L, 0.26mg/L, 0.25mg/L
and 0.35mg/L, respectively. In the results of amino acid composition of peak 1, peak 2, peak 3 and peak 4, it was observed that peak 1 was consisted mainly of glycine and methionine, peak 2 was proline, cystine and methionine, peak 3 was proline and peak 4 was alanine, methionine and leucine. In conclusion, beef heart hydrolysate treated with thermolysin+ proteinase A was shown to have the highest inhibitory effect for 12hrs incubation at 37.(

Mechanism of reaction of myeloperoxidase with hydrogen peroxide and chloride ion.

The reaction of myeloperoxidase compound I (MPO-I) with chloride ion is widely assumed to produce the bacterial killing agent after phagocytosis. Two values of the rate constant for this important reaction have been published previously: 4.7 x 106 M-1.s-1 measured at 25 degrees C [Marquez, L.A. and Dunford, H.B. (1995) J. Biol. Chem. 270, 30434-30440], and 2.5 x 104 M-1.s-1 at 15 degrees C [Furtmüller, P.G., Burner, U. & Obinger, C. (1998) Biochemistry 37, 17923-17930]. The present paper is the result of a collaboration of the two groups to resolve the discrepancy in the rate constants. It was found that the rate constant for the reaction of compound I, generated from myeloperoxidase (MPO) and excess hydrogen peroxide with chloride, decreased with increasing chloride concentration. The rate constant published in 1995 was measured over a lower chloride concentration range; the 1998 rate constant at a higher range. Therefore the observed conversion of compound I to native enzyme in the presence of hydrogen peroxide and chloride ion cannot be attributed solely to the single elementary reaction MPO-I + Cl- --> MPO + HOCl. The simplest mechanism for the overall reaction which fit the experimental data is the following: MPO+H2O2 &rlarr;k-1k1 MPO-I+H2O MPO-I+Cl- &rlarr;k-2k2 MPO-I-Cl- MPO-I-Cl- -->k3 MPO+HOCl where MPO-I-Cl- is a chlorinating intermediate. We can now say that the 1995 rate constant is k2 and the corresponding reaction is rate-controlling at low [Cl-]. At high [Cl-], the reaction with rate constant k3 is rate controlling. The 1998 rate constant for high [Cl-] is a composite rate constant, approximated by k2k3/k-2. Values of k1 and k-1 are known from the literature. Results of this study yielded k2 = 2.2 x 106 M-1.s-1, k-2 = 1.9 x 105 s-1 and k3 = 5.2 x 104 s-1. Essentially identical results were obtained using human myeloperoxidase and beef spleen myeloperoxidase.

Emergence of the active site of spleen exonuclease upon association of the two basic monomers of the tetrameric enzyme

The 5′→3′ exonuclease from beef spleen is a 160-kDa tetramer consisting of four subunits of two types. Partial reduction of the tetramer led to one stable intermediate state of the enzyme with M r=80 kDa. The aim of this paper was to attribute the exonucleolytic activity to one of the two monomers, to the dimer or to the tetramer. The different forms of the exonuclease were separated by SDS-polyacrylamide gel electrophoresis, transferred on an Immobilon-P membrane and subsequently renaturated. Antibodies monospecific against each of the two monomers as well as against the dimer were isolated and their inhibitory effect on the holoenzyme determined. It was found that after renaturation the two monomers did not possess any exonuclease activity while the 80-kDa dimer showed a lower recovery of the specific activity of the enzyme (20.8±0.23 nkat/nmol, ( n=5)) in comparison with the 160-kDa tetramer (64.8±0.75 nkat/nmol ( n=5)). It was demonstrated that the antibodies monospecific against the dimer caused 53% maximum inhibition of the 160-kDa exonuclease. The antibodies monospecific against 25- and 55-kDa monomers did not inhibit the activity of the holoenzyme. No single-strand endonuclease activity of the spleen exonuclease was observed when using supercoiled Bluescript KS+ plasmid DNA as a substrate. This data suggest the emergence of an 80 kDa active form of beef spleen exonuclease upon association of two monomers of the tetrameric enzyme.

The protective effect on Cu 2+- and AAPH-mediated oxidation of human low-density lipoproteins depends on glycosaminoglycan structure

The effect of various glycosaminoglycans on Cu 2+- and AAPH-induced oxidation of human low-density lipoprotein (LDL) was studied by monitoring conjugated diene formation. Heparin (Hep) increased the lag phase (t lag) of LDL oxidation, and fast moving and slow moving Hep species modified the kinetics of LDL oxidation to the same extent. Beef spleen heparan sulfate (HS) sample produced a significant increase of the t lag and a decrease of the conjugated diene formation of LDL whilst beef kidney HS species modified LDL oxidation kinetics to a lower extent. Dermatan sulfate (DS) from different sources caused a significant increase of the t lag and a decrease of the conjugated diene formation of LDL. Hyaluronic acid had no effect. Chondroitin sulfate (CS) from beef trachea produced a very strong protective antioxidant effect evaluated by increasing of the t lag and decreasing of the conjugated diene formation. Hep was completely ineffective in protecting LDL from 2,2'-azobis(2-amidinopropane) hydrochloride (AAPH)-mediated oxidation, whilst DS was moderately effective. Beef trachea CS showed a very strong ability to protect LDL oxidation induced by 1 mM AAPH. The different protective effect on Cu 2+- and AAPH-induced LDL oxidation by glycosaminoglycans is discussed considering their various structures and properties, and their capacity to interact to different extents with hydrophobic regions of LDL protein is confirmed by measuring the LDL-tryptophan fluorescence kinetics.

Reviewer bias against the unconventional? A randomized double-blind study of peer review

To test the hypothesis that there is a reviewer bias against publication of a test of an unconventional drug. Randomized, controlled, double-blind study of peer review. Convenience sample of 291 medical doctors from a wide variety of specialties drawn from a list of conference participants. Reviewers were randomly assigned to receive one of two versions of a manuscript. Version M related to an in-vitro experiment on a mainstream drug (Metoprolol). The otherwise identical version V used a highly unconventional drug (beef spleen cell extract) for the same experiment. Reviewers were asked to complete a standardised evaluation sheet including visual analogue scales (VASs) on a set of predefined quality criteria. All participants were debriefed after completion of the study. The response rate was 61%. There were no significant differences in VAS ratings between the two versions of the manuscript. Ratings covered the entire range of the VASs. In the present setting, there was no evidence for a reviewer-bias against testing an unconventional drug. The low inter-rater reliability, however, suggested inadequate validity of peer review.

Oligomeric Protein Structure of Beef Spleen Exonuclease

A one-step purification of beef spleen exonuclease in the form of a DNA–enzyme complex is described. The purity of the exonuclease was verified by two-dimensional gel electrophoresis. It possesses molecular mass 160 kDa and pI6.92. The one-dimensional sodium dodecyl sulfate gel after reduction with β-mercaptoethanol suggests that the 160-kDa exonuclease consists of four polypeptide chains of two different types with molecular masses 55 and 25 kDa. The tetrameric structure of the exonuclease is supported by intermolecular disulfide bonds, and their partial reduction leads to the formation of one stable intermediate with molecular mass 80 kDa formed by binding one 55-kDa with one 25-kDa subunit into a dimer. During two-dimensional gel electrophoresis, the dimer showed pI6.92 while monomers showed pI6.78 for the 55-kDa and pI6.29 for the 25-kDa. Two other intermediate states of two big and one small (135 kDa) and two small and one big subunit (105 kDa) were also visualized. They are unstable and easily dissociated into one 80-kDa dimer and either one 55-kDa or one 25-kDa monomer. The immunoblotting analysis with specific polyclonal antibodies against 160-kDa protein confirmed the subunit structure of the exonuclease. It was found that both monomers are glycosylated.

Studies on the Catalytic Mechanism of Pig Purple Acid Phosphatase

Several independent experiments failed to reveal any evidence in support of the involvement of a phosphoryl-enzyme intermediate in the catalytic mechanism of pig allantoic fluid purple acid phosphatase: (i) attempts to label enzyme with phosphate derived from [32P]p-nitrophenyl phosphate were unsuccessful; (ii) values of kcat for a series of phosphate derivatives varied over a wide range, with the enzyme showing a marked preference for activated ester and anhydride substrates over those with a stable leaving group; (iii) burst titrations revealed a "burst" of p-nitrophenol from p-nitrophenyl phosphate only when the enzyme was added after the substrate, suggesting that this result was an artifact of the order of addition of reagents; (iv) transphosphorylation from p-nitrophenyl phosphate to acceptor alcohols could not be detected, even under conditions where a transphosphorylation to hydrolysis ratio as low as 0.015 could have been measured; (v) enzyme-catalyzed exchange of 18O between phosphate and water was demonstrated, although at a rate much slower than that observed for other phosphatases where the involvement of a phosphoryl-enzyme intermediate in the mechanism has been clearly established. The present results are compared with those obtained in similar studies on other phosphatases, particularly the highly homologous beef spleen purple acid phosphatase, and their implications for the catalytic mechanism of the purple acid phosphatases are discussed.

Effects of Glycosaminoglycans on U-937 Leukemia Cell Proliferation and Differentiation: Structure-Function Relationship

Glycosaminoglycans (heparins, dermatan sulfate, chondroitin sulfate) with different structures and physicochemical properties were evaluated for their capacity to influence proliferation and differentiation of U-937 cell line. The contrasting and specific effects of glycosaminoglycans (depending on their structures and properties) on a leukemia cell line could help explain the regulation of proliferative and/or differentiative processes of hematopoietic cells in order to clarify the control of development and differentiation of hematopoietic progenitor cells by bone marrow extracellular matrix.Heparin from beef intestinal mucosa, heparan sulfate from beef spleen, dermatan sulfate from beef intestinal mucosa, and chondroitin sulfate from bovine trachea were extracted and purified, and their purity, structures, and physicochemical properties were evaluated. Fast-moving heparin was obtained by its selective precipitation as barium salt, and partially desulfated and re-N-sulfated heparin was produced by chemical modifications. Different glycosaminoglycans were tested to evaluate their effects on proliferation and differentiation processes of a monoblastic leukemia cell line (U-937).Heparin and derivatives (from 0.1 to 100 μg/ml) inhibit cell proliferation; heparan sulfate does not produce modifications, while chondroitin sulfate and dermatan sulfate (from 0.01 to 100 μg/ml) significantly stimulate cell growth.Cell differentiation was evaluated by cytoenzymatic determination of α-naphthyl butyrate esterase and by fluorescein-labeled anti-HLA-DR, anti-CD11b, and anti-CD14 antibodies. Nitro blue tetrazolium reduction and phagocytosis were also evaluated. Heparin and derivatives significantly increase U-937 differentiation. Heparin sulfate has no effect, while chondroitin sulfate and, to a lesser extent, dermatan sulfate, induce a strong decrease of differentiative markers.The regulation of U-937 cell properties appears to be related to charge density and to the amount of N-sulfate and N-acetyl groups. In particular, glycosaminoglycans with lower sulfate-to-carboxyl ratios and N -sulfate group percentages (chondroitin sulfate and dermatan sulfate) stimulate proliferation and produce a decrease of differentiative markers; on the contrary, polysaccharides with high charge density and N-sulfate group amounts (heparin and derivatives) inhibit U-937 proliferation and induce terminal differentiation.A previous paper (N. Volpi, L. Bolognani, A. Conte, and M. Petrini, (1993) Leukemia Res . 17, 789-798) demonstrates dissimilar effects on U-937 cells by chondroitin sulfates with different structures and physicochemical properties. In this study we confirm the importance of glycosaminoglycan structures and physicochemical properties in regulating cell functions. Possible mechanisms of action are discussed.

Comparative action of cathepsins B and L on intramuscular collagen as assessed by differential scanning calorimetry

Intramuscular beef collagen of different degrees of reticulation was treated with cathepsin L obtained from chicken liver and a commercial cathepsin B prepared from beef spleen. It was shown that, in the absence of calcium, both proteinases caused a decrease in the initial temperature of denaturation whereas the total enthalpy of denaturation was unaffected. Treatment with cathepsin B resulted in the appearance of a new peak of denaturation at a lower temperature (≈ 44°C), a change wholly comparable with that obtained previously when intramuscular beef collagen was treated with a collagenase from Clostridium histolyticum. There was no such change with cathepsin L. The addition of 20 mM CaCl 2 to the incubation buffer brought about a shift in the total enthalpy of denaturation when collagen was treated with cathepsin L; in contrast, no additional effect was observed in cathepsin B treatments. These findings led to the suggestion that cathepsins B and L have a different mode of action on collagen and that there may be a similarity in the mechanism of action between cathepsin B and the bacterial collagenase.

Cloning, sequence, and developmental expression of a type 5, tartrate-resistant, acid phosphatase of rat bone.

Tartrate-resistant acid phosphatase (TRAP) is a characteristic constituent of osteoclasts and some mononuclear preosteoclasts and, therefore, used as a histochemical and biochemical marker for osteoclasts and bone resorption. We now report the isolation of a 1397-base pair (bp) full-length TRAP/tartrate-resistant acid ATPase (TrATPase) cDNA clone from a neonatal rat calvaria lambda gt11 cDNA library. The cDNA clone consists of a 92-bp untranslated 5'-flank, an open reading frame of 981 bp and a 324-bp untranslated 3'-poly(A)-containing region. The deduced protein sequence of 327 amino acids contains a putative cleavable signal sequence of 21 amino acids. The mature polypeptide of 306 amino acids has a calculated Mr of 34,350 Da and a pI of 9.18, and it contains two potential N-glycosylation sites and the lysosomal targeting sequence DKRFQ. At the protein level, the sequence displays 89-94% homology to TRAP enzymes from human placenta, beef spleen, and uteroferrin and identity to the N terminus of purified rat bone TRAP/TrATPase. An N-terminal amino acid segment is strikingly homologous to the corresponding region in lysosomal and prostatic acid phosphatases. The cDNA recognized a 1.5-kilobase mRNA in long bones and calvaria, and in vitro translation using, as template, mRNA transcribed from the full-length insert yielded an immunoprecipitated product of 34 kDa. In neonatal rats, TRAP/TrATPase mRNA was highly expressed in skeletal tissues, with much lower (less than 10%) levels detected in spleen, thymus, liver, skin, brain, kidney, brain, lung, and heart. In situ hybridization demonstrated specific labeling of osteoclasts at endostal surfaces and bone trabeculae of long bones. Thus, despite the apparent similarity of this osteoclastic TRAP/TrATPase with type 5, tartrate-resistant and purple, acid phosphatases expressed in other mammalian tissues, this gene appears to be preferentially expressed at skeletal sites.

The first binuclear iron(III) complex with a terminally coordinated phosphato ligand—a model compound for the oxidized form of purple acid phosphatase from beef spleen

Reaction of N,N,N′,N′-tetrakis(2-benzimidazolylmethyl)-2-hydroxy-1,3-diaminopropane dihydrochloride (Htbpo·2HCl) with Fe(ClO4)3·9H2O and diphenylphosphate yields red crystals of [Fe2Cl2{O2P(OPh)2}(tbpo)(MeOH)](ClO4)2·3MeOH; the X-ray structure shows a phosphate ligand terminally coordinated to Fe(2) and a methanol ligand coordinated to Fe(1).

Meat By‐product Protein Composition and Functional Properties in Model Systems

ABSTRACTComposition and functional properties of selected meat by‐products were studied. Mechanically deboned chicken meat (MDCM) and meat by‐products (pork lung lobes, pork liver, beef lung lobes, beef spleen, beef heart) varied in their proximate composition, amount of the three major protein fractions [low ionic strength soluble (LIS), high ionic strength soluble (HIS), insoluble] and collagen content. Cooked batter model system reheat yield was positively correlated with the quantity of HIS proteins and the percentage myosin and actin in the HIS protein fraction. Stress and strain at failure of the cooked batters were inversely correlated to the amount of LIS proteins and positively correlated with the percentage of myosin and actin in the by‐products.

XAS investigations on purple acids phosphatases from red kidney beans and beef spleen

XAS investigations on purple acids phosphatases from red kidney beans and beef spleen

Identification of the FTBL protein of Sumner and Dounce as a leucine aminopeptidase

The crystalline beef liver protein of Sumner and Dounce (A. L. Dounce, P. Z. Allen, and G. A. Mourtzikos (1978) Arch. Biochem. Biophys. 188, 251–265 (1)) termed FTBL (football) protein because of the shape of its crystals, has been identified as a crystalline leucine aminopeptidase (LAP), on the basis of its high specific LAP activity and coincidence of its N terminal amino acid sequence (30 amino acids) with that of beef eye lens LAP. Amino acid analyses of the two proteins are also in reasonable agreement when based on the exact monomer molecular weight of beef eye lens protein obtained by the van Loon group ((1982) J. Biol. Chem. 257, 7077–7081) . Our previously published (1) monomer molecular weight of the FTBL protein was 25% too high, leading to the erroneous conclusion that the beef liver FTBL-LAP protein was a tetramer rather than a hexamer, as found by the van Loon group for beef lens LAP. The present report, taken together with our first paper on the FTBL protein establishes that the FTBL-LAP protein has been isolated from beef kidney and beef spleen as well as from beef liver. We now find that the properties of FTBL-LAP protein indicate that it is the same protein as beef eye lens LAP. The cellular and intracellular distributions of the FTBL-LAP protein have been considered in our first publication on the FTBL protein (1).

Sequence homology in the metalloproteins; Purple acid phosphatase from beef spleen and uteroferrin from porcine uterus

The primary structures of purple acid phosphatase and uteroferrin, two iron-binding glycoproteins isolated from beef spleen and porcine uterine fluids, respectively, have been examined by a combination of tandem mass spectrometry and classical Edman sequencing methods. Reported here are amino acid sequence data covering more than 90% of the primary structures for these two proteins. The sequence data reveal an unexpectedly high degree of homology, > 90%, for these two proteins.

ChemInform Abstract: X‐Ray Absorption Studies of the Purple Acid Phosphatase from Beef Spleen.

Chemischer InformationsdienstVolume 17, Issue 49 Physical Organic Chemistry ChemInform Abstract: X-Ray Absorption Studies of the Purple Acid Phosphatase from Beef Spleen. S. M. KAUZLARICH, S. M. KAUZLARICHSearch for more papers by this authorB. K. TEO, B. K. TEOSearch for more papers by this authorT. ZIRINO, T. ZIRINOSearch for more papers by this authorS. BURMAN, S. BURMANSearch for more papers by this authorJ. C. DAVIS, J. C. DAVISSearch for more papers by this authorB. A. AVERILL, B. A. AVERILLSearch for more papers by this author S. M. KAUZLARICH, S. M. KAUZLARICHSearch for more papers by this authorB. K. TEO, B. K. TEOSearch for more papers by this authorT. ZIRINO, T. ZIRINOSearch for more papers by this authorS. BURMAN, S. BURMANSearch for more papers by this authorJ. C. DAVIS, J. C. DAVISSearch for more papers by this authorB. A. AVERILL, B. A. AVERILLSearch for more papers by this author First published: December 9, 1986 https://doi.org/10.1002/chin.198649037AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinked InRedditWechat No abstract is available for this article. Volume17, Issue49December 9, 1986 RelatedInformation

X-ray absorption studies of the purple acid phosphatase from beef spleen

X-ray absorption studies of the purple acid phosphatase from beef spleen

The interaction of phosphate with the purple acid phosphatase from beef spleen: Evidence that phosphate binding is accompanied by oxidation of the iron chromophore

Reaction of the reduced (pink) form of the purple acid phosphatase from beef spleen with excess phosphate at pH 5.0, monitored by optical and low temperature EPR spectroscopy and by measurement of enzymatic activity, results in parallel loss of activity and oxidation of the iron chromophore. Colorimetric and radiochemical ( 32P) experiments indicate the presence of one mole of tightly bound phosphate in the oxidized (purple) form of the enzyme; this phosphate is released upon reduction. Acid hydrolysis of 32P-phosphate-containing enzyme, followed by high voltage paper electrophoresis, gave no evidence for significant amounts of acid-stable phosphoamino acids.