Analyze Diet

Topic:Enzymes

Enzymes are biological catalysts that facilitate biochemical reactions in horses by lowering the activation energy required for these processes. They are involved in various physiological functions, including digestion, metabolism, and cellular repair. Common enzymes in equine biology include amylase, lipase, and lactate dehydrogenase, each playing a specific role in the breakdown of nutrients and energy production. The activity and concentration of these enzymes can vary in response to different physiological and pathological conditions, serving as potential indicators in veterinary diagnostics. This page compiles peer-reviewed research studies and scholarly articles that explore the function, regulation, and clinical implications of enzymes in equine health.
Titration of antiserum to South American rattlesnake (Crotalus durissus terrificus) venom by measuring inhibition of phospholipase A2 activity.
Toxicon : official journal of the International Society on Toxinology    January 1, 1982   Volume 20, Issue 3 563-569 doi: 10.1016/0041-0101(82)90050-2
da Silva MH, Bier OG.Horse antiserum to the venom of Crotalus durissus terrificus, A South American rattlesnake, inhibits the phospholipase activity of the crude venom. There is a close relationship between this inhibitory property and the neutralizing potency of the antiserum in vivo. This may provide the basis for a rigorous standardization of anticrotalid venom in vitro.
Endotoxin-induced change in hemograms, plasma enzymes, and blood chemical values in anesthetized ponies: effects of flunixin meglumine.
American journal of veterinary research    January 1, 1982   Volume 43, Issue 1 140-144 
Fessler JF, Bottoms GD, Roesel OF, Moore AB, Frauenfelder HC, Boon GD.A study was made of flunixin meglumine (FM), an analgesic agent with antiprostaglandin activity, in the management of endotoxin-induced changes in ponies. Three groups of 5 ponies each were used: A--controls, B--nontreated ponies with endotoxin-induced shock, and C--ponies with endotoxin-induced shock treated with FM. Shock was induced in anesthetized ponies with IV injections of Escherichia coli endotoxin. Disruption of glucose homeostasis, insulin levels, hemograms, aerobic metabolism, and cell damage as indicated by plasma enzymes were observed. Treatment with FM (5 minutes) after shock was...
Metabolism of purine nucleosides and phosphoribosylpyrophosphate in thymocytes and splenocytes of various mammalian species.
Comparative biochemistry and physiology. B, Comparative biochemistry    January 1, 1982   Volume 73, Issue 3 535-541 doi: 10.1016/0305-0491(82)90071-2
Peters GJ, Oosterhof A, Veerkamp JH.1. Activities of ADA, PNP and AK were measured in splenocytes and thymocytes of newborn children, young horses, pigs, sheep, rats and mice and compared with the activities previously found in peripheral lymphocytes. 2. With all species, except horse, the activity of ADA (per 10(6) cells) was higher in thymocytes than in lymphocytes. Activity of ADA was highest in splenocytes of pig and sheep. Activity of ADA was lowest in all lymphoid cells of the horse and only about 10% of the activity in human splenocytes and lymphocytes. 3. With all species, except horse, the activity of PNP was lower in t...
Cibacron Blue-induced modification of neutral proteinase from horse blood leukocytes.
Acta biologica et medica Germanica    January 1, 1982   Volume 41, Issue 1 47-52 
Potempa J.The proteolytic activity of the elastase-like proteinase from granules of horse blood leukocytes is retained on a column of Cibacron Blue-Sepharose and can be eluted with 0.5 M KSCN. During this procedure its mol. wt. is reduced from 49000 to 30000 and isoelectric point is shifted towards higher pH. The inactive protein not adsorbed on Cibacron Blue-Sepharose is strongly acidic and shows a mol. wt. of 20000. Upon mixing this protein with the modified enzyme the native proteinase is reconstituted as shown by polyacrylamide gel electrophoresis at pH 8.3 and isoelectric focusing in a sucrose grad...
Immunodeficiency disease in animals.
Progress in clinical and biological research    January 1, 1982   Volume 94 271-307 
Perryman LE, Magnuson NS.Significant contributions to understanding the role of lymphocyte subpopulations in the immune response and to the characterization of immunodeficiencies in children have been achieved through study of animal models of immunodeficiency. Additional contributions can be made in two important areas. One is through identification of relevant, naturally-occurring models of adenosine deaminase deficiency and purine nucleoside phosphorylase deficiency. The second, and potentially more important contribution, would be the identification of the metabolic basis for existing immune deficiencies. The nece...
Limited trypsinolysis of porcine and equine colipases. Spectroscopic and kinetic studies.
Biochimica et biophysica acta    December 29, 1981   Volume 671, Issue 2 155-163 doi: 10.1016/0005-2795(81)90129-x
Rathelot J, Canioni P, Bosc-Bierne I, Sarda L, Kamoun A, Kaptein R, Cozzone PJ.Porcine and equine colipases have been submitted to mild tryptic digestion. Proteolysis occurs at the Arg5-Gly6 bond with the loss of the N-terminal pentapeptide. Studies of native and trypsin-treated colipases by circular dichroism and laser chemically induced dynamic nuclear polarization indicate that proteolysis induces conformational changes in the region of the tyrosine cluster. Experiments in the presence of phospholipid provide further evidence showing that these residues are in or close to the region of the protein interacting with aggregated lipids. Kinetic studies of the reaction of ...
Species specificity of estrogen biosynthesis in pregnancy. Immunochemical difference of placental NADPH-cytochrome c (P-450) reductase in human, baboon and horse.
Journal of steroid biochemistry    December 1, 1981   Volume 15 449-452 doi: 10.1016/0022-4731(81)90313-7
Osawa Y, Higashiyama T, Nakamura T.NADPH-cytochrome c (P-450) reductases from human placental aromatase II and from horse placental microsomes were solubilized and purified to show a single band of 83,000 daltons in SDS-polyacrylamide gel electrophoresis. Rabbits were immunized with purified human placental aromatase II NADPHcytochrome c (P-450) reductase. The resulting antibodies (Reduc-Ab) were used to examine the species specificity of estrogen biosynthesis and the reductase activity in humans, baboons, horses and rats. Rcduc-Ab suppressed androstenedione aromatase activity in human, baboon and horse placental microsomes wit...
Effects of aflatoxins in young ponies.
American journal of veterinary research    December 1, 1981   Volume 42, Issue 12 2162-2164 
Aller WW, Edds GT, Asquith RL.Sixteen clinically normal, healthy ponies were randomly assigned to 4 groups and given aflatoxin B1 in doses of 0.045, 0.030, 0.015, and 0 (control) mg/kg of body weight per day for 21 days (or total doses of 0.945, 0.630, 0.315, and 0 mg/kg). The animals were allowed to recover for 3 months and then were reassigned to 4 treatment groups such that each group during the 2nd trial included a pony from each of the groups of the 1st trial. The animals in the new groups were intubated and were given aflatoxin in doses of 0.4, 0.2, 0.1, and 0 (control) mg/kg/day for 5 days ( or total doses of 2.0, 1...
Distribution of 5′-nucleotidase and gamma glutamyl transferase activities in the tissues of the horse.
Research in veterinary science    November 1, 1981   Volume 31, Issue 3 312-314 
Ford EJ, Adam SE.In the horse, 5'-nucleotidase (5'-NT) activity is found mainly in homogenates of lung, kidney, small intestine, mammary gland, liver and pancreas. Lower activities are present in brain and muscle. Activity can be demonstrated histochemically in the glomeruli and tubules of the kidney, in the sinusoidal borders of the hepatocytes and the bile duct epithelium as well as in the blood vessels of all organs. There is no significant difference between the 5'-NT activity in serum and plasma of normal horses and of horses suffering from a range of orthopaedic conditions. Previous findings that gamma g...
Primary structure of 3-phosphoglycerate kinase from horse muscle. I. Purification of cyanogen bromide peptides and amino acid sequence of peptide CB5 (104 residues).
The Journal of biological chemistry    October 25, 1981   Volume 256, Issue 20 10284-10292 
Hardy GW, Darbre A, Merrett M.3-Phosphoglycerate kinase was isolated from horse muscle and subjected to the action of cyanogen bromide. The resulting peptides were separated using gel filtration combined with either ion exchange chromatography on phosphocellulose in 6 M urea or high voltage paper electrophoresis. The sequence of the largest peptide, CB5, has been determined by a combination of automated and manual Edman degradation carried out on the intact peptide and derivatives obtained by proteolytic digestion. The isolation of two peptides derived from CB5 by cleavage of the bond between Asp109 and Pro110 facilitated ...
Analysis of the potentiometric titration of reduced horse heart cytochrome c.
Biopolymers    October 1, 1981   Volume 20, Issue 10 2243-2252 doi: 10.1002/bip.1981.360201016
Marini MA, Martin CJ, Forlani L.No abstract available
Mobilization of iron from ferritin by isolated mitochondria. Effects of species compatibility between ferritin and mitochondria and iron content of ferritin.
Biochimica et biophysica acta    September 18, 1981   Volume 677, Issue 1 50-56 doi: 10.1016/0304-4165(81)90144-6
Ulvik RJ, Romslo I, Roland F, Crichton RR.Mitochondria mobilize iron from ferritin by a mechanism that depends on external FMN. With rat liver mitochondria, the rate of mobilization of iron is higher from rat liver ferritin than from horse spleen ferritin. With horse liver mitochondria, the rate of iron mobilization is higher from horse spleen ferritin than from rat liver ferritin. The results are explained by a higher affinity between mitochondria and ferritins of the same species. The mobilization of iron increases with the iron content of the ferritin and then levels off. A maximum is reached with ferritins containing about 1 200 i...
Variations of plasma enzymes in the pony and the dog after carbon tetrachloride administration.
American journal of veterinary research    August 1, 1981   Volume 42, Issue 8 1461 
Easley JR.No abstract available
Biochemical changes in equine erythrocytes during experimental regenerative anemia.
The Cornell veterinarian    July 1, 1981   Volume 71, Issue 3 280-287 
Shull RM.Hemolytic or blood loss anemia was induce in six ponies and red blood cell concentrations of creatine, glucose-6-phosphate dehydrogenase (G-6-PD), lactate dehydrogenase (LDH), and aspartate transaminase (AST) were measured during the ensuing regenerative period. Creatine and G-6-PD levels correlated well and increased concentration of either was good indication of increased erythrogenesis. Erythrocyte LDH levels were of value in assessing the response to hemolytic anemia but not to blood loss anemia. The difference may be, at least in part, the result of differing degrees of regenerative effor...
Electron transfer between horse heart and Candida krusei cytochromes c in the free and bound states.
Biochimica et biophysica acta    July 1, 1981   Volume 636, Issue 2 129-135 doi: 10.1016/0005-2728(81)90085-2
Yoshimura T, Sogabe T, Aki K.Electron transfer between horse heart and Candida krusei cytochromes c in the free and phosvitin-bound states was examined by difference spectrum and stopped-flow methods. The difference spectra in the wavelength range of 540-560 nm demonstrated that electrons are exchangeable between the cytochromes c of the two species. The equilibrium constants of the electron transfer reaction for the free and phosvitin-bound forms, estimated from these difference spectra, were close to unity at 20 degrees C in 20 mM Tris-HCl buffer (pH 7.4). The electron transfer rate for free cytochrome c was (2-3).10(4)...
Nucleic acid-protein interactions. Degradation of double-stranded RNA by glycosylated ribonucleases.
Biochimica et biophysica acta    June 26, 1981   Volume 654, Issue 1 77-85 doi: 10.1016/0005-2787(81)90138-6
Carsana A, Furia A, Gallo A, Beintema JJ, Libonati M.1. Extensively glycosylated ribonucleases, like the enzymes from pig and horse pancreas, show a much higher activity on double-stranded RNAs than similarly charged, carbohydrate-free RNAases under stranded assay conditions (relatively high salt concentrations). Glycosylated pig and horse pancreas RNAases also show a larger destabilizing effect on double-stranded poly[d(A-T)] X poly[d(A-T)], than that displayed by bovine RNAase A under these conditions. Both activities show a similar dependence on the ionic strength of the medium. 2. A partial enzymic removal of the heterosaccharide side chains...
Crystallization and properties of creatine kinase from equine skeletal muscle.
Journal of biochemistry    May 1, 1981   Volume 89, Issue 5 1619-1631 doi: 10.1093/oxfordjournals.jbchem.a133357
Takasawa T, Fukushi K, Shiokawa H.A crystalline creatine kinase was obtained from equine skeletal muscle. The enzyme was homogeneous, as judged by ultracentrifugation and disc electrophoresis on polyacrylamide gel. The crystalline enzyme had a specific activity of 110 units per mg of protein, that is, 14-fold purification over the crude extract of equine skeletal muscle. The molecular weight of the enzyme was determined to be 84,600 by the conventional low-speed sedimentation equilibrium method, and s020,w was 5.32S. Eight cysteine residues were found on amino acid analysis, two of which were essential for the enzymatic activi...
Origin an importance of increased alkaline phosphatase activity in peritoneal fluids of horses with colic.
American journal of veterinary research    May 1, 1981   Volume 42, Issue 5 888-891 
Froscher BG, Nagode LA.The origin of increased alkaline phosphatase (ALP) activity in peritoneal fluid (PF) of horses with clinical signs of abdominal pain was investigated to determine the usefulness of measuring ALP in PF in the diagnosis of small intestinal injury. The ALP isoenzymes in PF from 10 clinically normal horses and from 50 horses with clinical signs of acute abdominal pain were analyzed for their sensitivities to inhibition by L-phenylalanine, L-homoarginine, and levamisole and to inactivation by heat (56 C, 15 minutes). The enzymes also were discriminated by their patterns of migration during polyacry...
Hydrolysis by horse muscle acylphosphatase of (Ca2+ + Mg2+)-ATPase phosphorylated intermediate.
Archives of biochemistry and biophysics    April 15, 1981   Volume 208, Issue 1 37-41 doi: 10.1016/0003-9861(81)90120-x
Stefani M, Liguri G, Berti A, Nassi P, Ramponi G.No abstract available
Variations of plasma enzymes in the pony and the dog after carbon tetrachloride administration.
American journal of veterinary research    April 1, 1981   Volume 42, Issue 4 674-678 
Noonan NE.Adult female dogs or pony mares were subjected to a nonlethal dose of CCl4 (0.5 ml/kg of body weight). Amounts of several plasma enzymes thought to be indicative of hepatic disease were monitored. Plasma enzymes alanine aminotransferase, aspartate aminotransferase (AST), alkaline phosphatase (ALP), arginase, gamma-glutamyltransferase (GGT), and iditol dehydrogenase (ID), as well as total plasma bilirubin, were determined in these animals before and after the administration of the CCl4. In the dog, GGT was not significantly increased, whereas ALP values were increased during days 1 to 6. In the...
[Methods for the evaluation of the intestinal function in the horse (author’s transl)].
Nordisk veterinaermedicin    April 1, 1981   Volume 33, Issue 4-5 172-177 
Dietz HH.Diagnostic tests in horses showing signs of gastrointestinal diseases are reviewed. The use of rectal exploration is emphasized, and paracentesis as a diagnostic aid is mentioned. Special attention is given to the absorption tests as they are easy to conduct and give a relative measure of the absorptive capability of the intestinal epithelium. Glucose, D(+)-xylose and carbohydrate digestion-absorption tests are compared, and the D(+)-xylose absorption test is preferred because of the univocal curve of absorption (see Figure 1 and 2). The absorption curve in a horse suffering from alimentary ly...
Stabilization of the C-terminal part of pig and horse colipase by carboxypeptidase and trypsin inhibitors.
European journal of biochemistry    March 16, 1981   Volume 115, Issue 1 99-105 doi: 10.1111/j.1432-1033.1981.tb06203.x
Chapus C, Desnuelle P, Foglizzo E.Pig and horse colipases have been purified by a common procedure using trypsin and carboxypeptidase inhibitors as stabilizers. Two forms of pig colipase were identified: a predominant A1 form with about 103-105 residues, and a minor slightly degraded A2 form in which the last two C-terminal residues, Asp and Ser, were lacking. This type of degradation is considerably slowed down by carboxypeptidase inhibitors. A total of four forms of the horse cofactor were characterized: two (A1 and B1) were probably isocolipases which differed by only a few substitutions. Both contained the same number of r...
The cleavage of the Met-Lys bond in a bradykinin derivative by glandular kallikreins.
Hoppe-Seyler's Zeitschrift fur physiologische Chemie    March 1, 1981   Volume 362, Issue 3 337-345 doi: 10.1515/bchm2.1981.362.1.337
Araujo-Viel MS, Juliano L, Prado ES.The synthetic tridecapeptide Gly-Leu-Met-Lys-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg was used as a model substrate for horse urinary and porcine pancreatic kallikreins. The Met-Lys bond is hydrolyzed selectively by both enzymes. Oxidation of the methionine residue to sulfoxide made the peptide resistant to both kallikreins. Substitution of either the methionine or lysine residues by norleucine led to peptides in which the Nle-Lys or the Met-Nle bonds, respectively, were susceptible to the urinary kallikrein. The esterolytic and Met-Lys bond-splitting activities of both enzymes were inhibited simil...
Physico-chemical properties of pregnant mare serum gonadotropin.
Biochimica et biophysica acta    February 27, 1981   Volume 667, Issue 2 267-276 doi: 10.1016/0005-2795(81)90192-6
Combarnous Y, Salesse R, Garnier J.Pregnant mare serum gonadotropin exhibits a dissociation at acid pH as shown by the drop of s20,w values from 3.52 S at pH 8.1 to 2.52 S at pH 2.0. The dissociation is accompanied by an absorbance change with a maximum at 287 nm and a parallel loss of both follicle-stimulating hormone (FSH) and luteinizing hormone (LH) activities as followed by radioreceptor assays. The apparent pKa of the acid transition is 3.45 with an extremely slow and temperature-dependent rate at pH 2.0 (1.8 . 10(-4) s-1 at 37 degrees C). By gel filtration the molecular weight of the active hormone is estimated to be 45 ...
Activation of pigeon erythrocyte adenylate cyclase by cholera toxin. Partial purification of an essential macromolecular factor from horse erythrocyte cytosol.
Biochimica et biophysica acta    February 5, 1981   Volume 672, Issue 3 248-261 doi: 10.1016/0304-4165(81)90291-9
Le Vine H, Cuatrecasas P.A cytosolic, macromolecular factor required for the cholera toxin-dependent activation of pigeon erythrocyte adenylate cyclase and cholera toxin-dependent ADP-ribosylation of a membrane-bound 43,000 dalton polypeptide has been purified 1100-fold from horse erythrocyte cytosol using organic solvent precipitation and heat treatment. This factor, 13,000 daltons, does not absorb to anionic or cationic exchange resins, is sensitive to trypsin or 10% trichloroacetic acid and is not extractable by diethyl ether. Activation of adenylate cyclase by cholera toxin requires the simultaneous presence of AT...
Rapid-scanning spectral evidence for catalytically nonequivalent but interconvertible forms of equine liver alcohol dehydrogenase.
Biochimie    February 1, 1981   Volume 63, Issue 2 97-102 doi: 10.1016/s0300-9084(81)80171-x
Koerber SC, Dunn MF.These rapid-scanning stopped-flow kinetic studies of the equine liver alcohol dehydrogenase-catalyzed reduction of p-nitrobenzaldehyde by NADH and (4R)-4-deuterio NADH (NADD) under single turnover conditions establish : (1) The reaction is biphasic using NADD as coenzyme, k1 approximately 200 sec-1, k2 = 0.5 sec-1 and the amplitude ratio (A1)/(A1 + A2) approximately equal to 0.5. (2) Each phase of the reaction involves the oxidation of enzyme-bound reduced coenzyme. (3) The recycling of sites in the presence of 20 mM pyrazole is negligible. (4) The rates of E(NAD-pyrazole) complex formation at...
Fibrinolytic activity without fibrinogenolysis during long-distance racing in horses.
Journal of applied physiology: respiratory, environmental and exercise physiology    February 1, 1981   Volume 50, Issue 2 245-249 doi: 10.1152/jappl.1981.50.2.245
Ferguson EW, Bernier LL, Shaughness GP, Boucher JH.Fourteen horses were studied during a 157-km endurance ride. Two humans who ran the 157 km were also evaluated at the finish. Fibrin monomer samples were examined by two-dimensional gel electrophoresis and sodium dodecyl sulfate polyacrylamide gel electrophoresis. Two major species of horse Beta-chain with higher molecular weights and different isoelectric mobilities than human beta-chain were observed. Horse alpha-chains had higher molecular weights than human alpha-chains but similar alpha-chain heterogeneities. Mean euglobulin lysis time (ELT) in the horses was accelerated to similar levels...
Alcohol dehydrogenase from Leuconostoc mesenteroides: molecular properties in comparison with the yeast and horse liver enzyme.
The International journal of biochemistry    January 1, 1981   Volume 13, Issue 12 1215-1224 doi: 10.1016/0020-711x(81)90067-7
Schneider-Bernlöhr H, Fiedler H, Gerber M, Weber C, Zeppezauer M.No abstract available
Predicted secondary structure of horse muscle acylphosphatase. Comparison with circular dichroism measurements.
Physiological chemistry and physics    January 1, 1981   Volume 13, Issue 3 267-273 
Camici G, Manao G, Cappugi G, Ramponi G.We have predicted the secondary structure of horse muscle acylphosphatase by the statistical method of Chou and Fasman. In addition, we have studied the circular dichroism spectra of the enzyme, obtaining values for comparison to the predicted results. Discrepancies were found for the alpha-helix content estimated by the two methods.
[Localization of beta-n-acetylhexosaminidase in stallion epididymis (author’s transl)].
Acta histochemica    January 1, 1981   Volume 69, Issue 1 77-84 
Skolek-Winnisch R, Lipp W, Stöckl W, Bamberg E.The localization of beta-N-acetylhexosaminidase activity in 6 different segments of the epididymis was investigated in 8 stallions using biochemical and histochemical methods. The highest enzyme activity was found in segment D while the other segments displayed a much weaker reaction There was no or only low enzyme activity present in the epididymal fluid of the proximal 3 segments, whereas it was high in the distal 3 segments. The biological function of beta-N-acetylhexosaminidase in the epididymis is discussed briefly.
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