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.
Mammalian erythrocyte glutathione reductase: kinetic constants and saturation with cofactor.
American journal of veterinary research    October 1, 1975   Volume 36, Issue 10 1511-1513 
Harvey JW, Kaneko JJ.Glutathione reductase (GR) was studied in erythrocytes of horses, cats, dogs, and man. Glutathione reductase activity was measured in hemolysates with and without preincubation of hemolysates with flavinadenine dinucleotide. The percentage saturation of GR apoenzyme with cofactor (flavin-adenine dinucleotide) was lower in cats and dogs than in horses or man. The greatest amount of inactive apoenzyme was in feline erythrocytes. Total GR activity listed in order by species is cat greater than man greater than dog greater than horse. Kinetic constants for oxidized glutathione and reduced nicotina...
Horse liver alcohol dehydrogenase. A study of the essential lysine residue.
The Biochemical journal    September 1, 1975   Volume 149, Issue 3 627-635 doi: 10.1042/bj1490627
Chen SS, Engel PC.1. The inactivation of horse liver alcohol dehydrogenase by pyridoxal 5'-phosphate in phosphate buffer, pH8, at 10 degrees C was investigated. Activity declines to a minimum value determined by the pyridoxal 5'-phosphate concentration. The maximum inactivation in a single treatment is 75%. This limit appears to be set by the ratio of the first-order rate constants for interconversion of inactive covalently modified enzyme and a readily dissociable non-covalent enzyme-modifier complex. 2. Reactivation was virtually complete on 150-fold dilution: first-order analysis yielded an estimate of the r...
[Ultrastructural and enzyme studies on trained and untrained horse muscles].
Schweizer Archiv fur Tierheilkunde    August 1, 1975   Volume 117, Issue 8 453-457 
Straub R, Howald H, Gerber H, Diehl M, Pauli B.No abstract available
ATPase activity and filament formation of partially purified myosin from leucocytes.
Journal of biochemistry    July 1, 1975   Volume 78, Issue 1 93-103 
Takeuchi K, Shibata N, Senda N.Myosin was isolated from leucocytes in horse arterial blood by the same procedures used for the isolation of myosin from skeletal muscle. The Ca2+-, EDTA-, and Mg2+-ATPase [EC 3.6.1.3] activities of the protein was 0.148, 0.147, and 0.001 mumoles/min/mg, respectively, in 0.5 M KCl at pH 7.0 and 25 degrees. The Ca2+-ATPase activity decreased with decrease in the ionic strength. No difference was found between leucocyte myosin and skeletal myosin in the pH profiles of Ca2+- and EDTA-ATPases. The rate and amount of the initial burst of Pi liberation of leucocyte myosin were 0.002 mumoles/min/mg a...
The influence of exercise on serum enzyme levels in the horse.
Equine veterinary journal    July 1, 1975   Volume 7, Issue 3 160-165 doi: 10.1111/j.2042-3306.1975.tb03258.x
Anderson MG.A group of clinically normal horses was subjected to controlled strenuous exercise. Elevated serum concentrations of lactic dehydrogenase, aldolase and creatine kinase were observed after exercise but no significant change in serum glutamic-oxalacetic transaminase was noted. These changes were reduced by repeated exposure to exercise suggesting that measurement of serum enzyme elevations, particularly creatine kinase, might be a useful index of fitness in the horse. Administration of prednisolone prior to exercise also reduced these changes. Since the serum enzyme concentrations had returned t...
Inhibition of horse muscle acylphosphatase by pyridoxal 5′-phosphate.
Biochimica et biophysica acta    June 24, 1975   Volume 391, Issue 2 486-493 doi: 10.1016/0005-2744(75)90272-7
Ramponi G, Manao G, Camici G, White GF.It has been shown that horse muscle acylphosphatase is inhibited by pyridoxal 5'-phosphate and that the inhibition is pH dependent, reversible and competitive with respect to substrate binding. Spectral analysis on the EI complex demonstrates the presence of a Schiff base. Reduction of the pyridoxal 5'-phosphate-inhibited enzyme with sodium borohydride, followed by amino acid analysis, produces a diminution of the free lysine peak and the appearance of a new peak corresponding to epsilon-pyridoxyllysine. The results suggest that there is at least one NH2-lysyl residue of horse muscle acylphosp...
Heat stability and reactivation of mare milk lysozyme.
Journal of dairy science    June 1, 1975   Volume 58, Issue 6 835-838 doi: 10.3168/jds.S0022-0302(75)84646-7
Jauregui-Adell J.Mare milk and aqueous solution of mare milk lysozyme were incubated for variable times between 30 C and 100 C at pH 3, 6, or 9. Lysozyme activity was stable at acid and neutral pH and labile at alkaline pH. Some of the results show the existence of a reactivation process in mare's milk and in aqueous solution. reaching 30 to 40% after incubation of the aqueous solution at 4 C for 20 days at pH 3 or 6.
Carboxymethyl horse-liver alcohol dehydrogenase. Ligand-binding and kinetic properties of the cysteine-46-modified enzyme.
Archives of biochemistry and biophysics    May 1, 1975   Volume 168, Issue 1 145-162 doi: 10.1016/0003-9861(75)90237-4
Reynolds CH, McKinley-McKee JS.No abstract available
Carboxylesterases (EC 3.1.1). Purification and titration of chicken, sheep, and horse liver carboxylesterases.
Canadian journal of biochemistry    May 1, 1975   Volume 53, Issue 5 536-546 doi: 10.1139/o75-074
Inkerman PA, Scott K, Runnegar MT, Hamilton SE, Bennett EA, Zerner B.Chicken, sheep, and horse liver carboxylesterases have been purified by procedures involving ammonium sulfate fractionation, ion-exchange chromatography and gel filtration on Sephadex. The actual yields of the procedures described were as follows: chicken, 1 g from 2 kg of liver powder (chloroform-acetone); sheep, 200 mg from 400 g of powder (chloroform-acetone); horse, 230 mg from 800 g of powder (acetone). The purified enzymes are free of non-carboxyl-esterase protein as shown by gel electrophoresis, although they do contain electrophoretic variants. The equivalent weight of the chicken enzy...
The different activities of arginase, arginine synthetase, ornithine transcarbamoylase and delta-ornithine transaminase in the liver and blood cells of some farm animals.
Comparative biochemistry and physiology. B, Comparative biochemistry    April 15, 1975   Volume 50, Issue 4 555-558 doi: 10.1016/0305-0491(75)90088-7
Owczarczyk B, Barej W.No abstract available
An examination of octanol and octanal metabolism to octanoic acid by horse liver alcohol dehydrogenase.
Biochimica et biophysica acta    March 28, 1975   Volume 384, Issue 1 1-11 doi: 10.1016/0005-2744(75)90090-x
Hinson JA, Neal RA.The kinetics of the horse liver alcohol dehydrogenase (alcohol: NAD+ oxidoreductase EC 1.1.1.1) catalyzed metabolism of octanol and octanal to octanoic acid have been examined. On incubation of octanol with horse liver alcohol dehydrogenase in the presence of NAD+, NADH as well as octanal and octanoic acid were seen as the initial products. However, on continued incubation, the octanal concentration progressively decreased to where only negligible quantities were present in the incubation after 10 min. The production of NADH was biphasic. An initial phase was followed in about 2 min with a slo...
Species variability in the modification of erythrocyte surface proteins by enzymatic probes.
Biochimica et biophysica acta    March 13, 1975   Volume 382, Issue 2 181-192 doi: 10.1016/0005-2736(75)90176-5
Carraway KL, Colton DG, Shin BC, Triplett RB.Bovine and equine erythrocytes have been studied by three different surface modification techniques to investigate the accessibility of the surface components to the external medium. Lactoperoxidase labeling of equine erythrocytes results in a significant labeling of only one membrane component, a 100 000-mol.wt polypeptide corresponding to the membrane-spanning Component III of human erythrocytes. The major sialoglycoprotein of the equine erythrocyte is not labeled. This is in contradistinction to the situation for human and bovine cells, where both components are labeled. The equine membrane...
Mercuri-nitrophenol as a reporter group for the conformational change of hemoglobin.
Journal of biochemistry    March 1, 1975   Volume 77, Issue 3 595-604 doi: 10.1093/oxfordjournals.jbchem.a130761
Yagisawa S.One mole of horse hemoglobin tetramer reacts with 2 moles of 2-chloromercuri-4-nitrophenol (MNP) at beta 93 cysteine. The difference spectra between NMP-bound hemoglobin and hemoglobin, measured with the aid of ascorbic acid and ascorate oxidase [EC 1.10.3.3] as deoxygenation reagents, indicate that the pK of the phenolic hydroxyl group of MNP increases by 0.6 to 0.8 pH unit on deoxygenation of the hemoglobin. The Hill constant of the modified hemoglobin changes with pH. It decreases from about 2.4 at pH 6.8 to about 1.0 at pH 9.0 This effect of the reagent is interpreted as inherent to the re...
Carbohydrate digestion and absorption in the equine small intestine.
Journal of the South African Veterinary Association    March 1, 1975   Volume 46, Issue 1 19-27 
Roberts MC.Dietary carbohydrates, which constitute a most important source of equine nutrition, are digested and absorbed by a series of complex processes principally in the small intestine, beginning with intraluminal starch hydrolysis by the action of pancreatic amylase. The continuous secretion of a copious volume of pancreatic juice, low in enzyme activity, presumably releases sufficient oligosaccharides for further hydrolysis at the intestinal cell surface by brush border enzymes. Active carrier mediated mechanisms then transport the final hexose products across the intestinal cell for uptake in the...
Identification of the lysine residue modified during the activation of acetimidylation of horse liver alcohol dehydrogenase.
Biochemistry    January 28, 1975   Volume 14, Issue 2 200-203 doi: 10.1021/bi00673a002
Dworschack R, Tarr G, Plapp BV.A single amino group in horse liver alcohol dehydrogenase was modified with methyl(14C)acetimidate by a differential labeling procedure. Lysine residues outside the active site were modified with ethyl acetimidate while a lysine residue in the active site was protected by the formation of an enzyme-NAD+-pyrazole complex. After the protecting reagents were removed, the enzyme was treated with methyl(14C)acetimidate. Enzyme activity was enhanced 13-fold as 1.1 (14C)acetimidyl group was incorporated per active site. A labeled peptide was isolated from a tryptic-chymotryptic digest of the modified...
Binding of Au(CN)2- and Pt(CN)4-2- to horse liver alcohol dehydrogenase. A 35C1NMR relaxation study.
Biochimica et biophysica acta    January 23, 1975   Volume 377, Issue 1 1-8 doi: 10.1016/0005-2744(75)90279-x
Bull TE, Lindman B, Einarsson R, Zeppezauer M.The binding of Au(CN)2- and Pt(CN)4-2- ions to the coenzyme binding site of horse liver alcohol dehydrogenase (alcohol : NAD+ oxidoreductase EC 1.1.1.1) has been studied by 35C1 nuclear magnetic relaxation. Longitudinal relaxation rates were analyzed in terms of a simple model and binding constants for Au(CN)2-, Pt(CN)4-2- and C1- were estimated. From a comparison between transverse and longitudinal relaxation rates the correlation time and the quadrupole coupling constant of bound chloride ion were obtained. The quadrupole coupling constant estimated from a simple electrostatic model for chlo...
[Comparative study of the optimum pH value of serum alkaline phosphatase in various species of farm animals].
Veterinarno-meditsinski nauki    January 1, 1975   Volume 12, Issue 6 89-93 
Goranov Kh, Ivanov V.Investigations were carried out on the alkaline phosphatase in the sera of cattle, horses, pigs, sheep, goats, and chickens, the pH value of the buffer used being 9.0-9.8-10.0-10.2-10.6 and 11.0, and the method applied--that of Richterich. The pH value at which the serum alkaline phosphatase in the various farm animals and birds was most active was found to vary to a large extent. Optimal values for the enzyme's activity usually range as follows: cattle, 10.2; pigs and goats, 10.0; sheep,--10.2; horses,--9.8; chickens,--10.6.
The multiple forms of acid phosphatase from horse leucocytes.
Bulletin de l'Academie polonaise des sciences. Serie des sciences biologiques    January 1, 1975   Volume 23, Issue 3 153-159 
Wasyl Z.No abstract available
[An immunologic study of hyaluronidase of different animal origin].
Veterinarno-meditsinski nauki    January 1, 1975   Volume 12, Issue 2 31-38 
Kozhukharova L.Studied was the antigenic relatedness of hyaluronidase contained in the semen of breeder animals of homologic and heterologic species. The experiments were carried out by means of the immunodiffusion and the immunoelectrophoretic methods. The results obtained showed that the seminal hyaluronidase of bulls, rams and bucks is antigenically related, and that of stallions, boars and rabbits does not exhibit antigenic relatedness. Stallion semen is closely related antigenically with the above-mentioned three animal species' semen as manifested by two precipitation bands, but these are not identical...
Immunological characteristics of proteins and enzymes from plasma of full stallion semen.
Bulletin de l'Academie polonaise des sciences. Serie des sciences biologiques    January 1, 1975   Volume 23, Issue 11 761-764 
Balbierz H, Bielański W, Kosiniak K, Nikolajczuk M.No abstract available
Carbohydrate digestion and absorption studies in the horse.
Research in veterinary science    January 1, 1975   Volume 18, Issue 1 64-69 
Roberts MC.The ability of the horse to digest and absorb soluble carbohydrates was assessed using a series of oral disaccharide tolerance tests followed in the same animals by tolerance tests with the constituent monosaccharides. In horses older than three years, lactose did not produce an increase in the plasma glucose levels but induced the passing of soft faeces, indicating that adult horses are lactose intolerant. Horses of all ages could absorb the glucose: galactose mixture without any change in the faeces. The tolerance is due to a failure to hydrolyse lactose and does not involve the monosacchari...
Immunological characteristics of proteins and enzymes from glandular secretions of particular segments of the reproductive organ in stallions.
Bulletin de l'Academie polonaise des sciences. Serie des sciences biologiques    January 1, 1975   Volume 23, Issue 12 833-837 
Balbierz H, Bielański W, Kosiniak A, Nikolajczuk M.No abstract available
The use of steady-state treatment in the rapid kinetics of horse liver alcohol dehydrogenase. The evaluation of data on the amplitude of the “burst” reaction.
Archives of biochemistry and biophysics    January 1, 1975   Volume 166, Issue 1 16-24 doi: 10.1016/0003-9861(75)90359-8
Tatemoto K.No abstract available
Enzyme activity in the serum of thoroughbred horses in the United Kingdom.
Equine veterinary journal    January 1, 1975   Volume 7, Issue 1 34-39 doi: 10.1111/j.2042-3306.1975.tb03226.x
Blackmore DJ, Elton D.This paper records the concentrations of aspartate amino transferase (A.A.T.), creatine kinase (C.P.K.), sorbitol dehydrogenase (S.D.H.), alpha-hydroxybuturate dehydrogenase (alpha-H.B.D.) and alkaline phosphatase (A.P.) activity observed in the sera of Thoroughbred horses in the United Kingdom, at rest and during training. The methods of analysis have been selected to achieve the optimum precision when used for horse serum. During training A.A.T., C.P.K. and alpha-H.B.D. are related and demonstrate intermittent periods of increasing activity. S.D.H. remains unchanged but demonstrates increase...
Immunological characteristics of proteins and enzymes from semen plasma of stallions collected fractionwise.
Bulletin de l'Academie polonaise des sciences. Serie des sciences biologiques    January 1, 1975   Volume 23, Issue 11 765-766 
Balbierz H, Bielański W, Kosiniak K, Nikolajczuk M.No abstract available
The application of polyvalent horse immune sera for electroimmunodiffusion methods.
Annales immunologiae Hungaricae    January 1, 1975   Volume 18 109-113 
Péterfy F, Varró R, Fatrai Z, Barna I, Kiss I.Horse immune sera do not give satisfactory results in immunochemical techniques based on electrophoresis of antigens through antibody-containing agarose gel. As the majority of precipitating horse antibodies belongs to the beta globulins, they migrate in the gel during electrophoresis. After enzymatic treatment the pepsin fragments work well in all electroimmunodiffusion methods.
Molecular properties of multiple forms of acid phosphatase from horse liver.
Acta biochimica Polonica    January 1, 1975   Volume 22, Issue 3 201-209 
Wasyl Z.1. Horse liver acid phosphatase was separated into two partially purified fractions differing in molecular weight (enzyme I about 100 00, enzyme II about 25 000). 2. Enzyme I was separated into several subfractions by DEAE-cellulose chromatography and isoelectric focusing. 3. Molecular weight, sedimentation coefficient and effective molecular radii were determined for acid phosphatases I and II by gel filtration and density-gradient centrifugation.
[Glutamic-oxaloacetic transaminase in stallion semen and its relation to other qualities of the spermatozoa. 2. Effect of castration on GOT contenet of stallion ejaculate].
Zuchthygiene    December 1, 1974   Volume 9, Issue 4 170-171 
Hillmann KH, Treu H.No abstract available
[Glutamic-oxaloacetic transaminase in stallion semen and its relation to other qualities of the spermatozoa. 3. Relation between various properties of stallion’s sperm].
Zuchthygiene    December 1, 1974   Volume 9, Issue 4 172-177 
Hillmann KH, Treu H.No abstract available
The purification of cholinesterase from horse serum.
The Biochemical journal    December 1, 1974   Volume 143, Issue 3 733-744 doi: 10.1042/bj1430733
Main AR, Soucie WG, Buxton IL, Arinc E.A relatively simple method is described by which cholinesterase was purified about 19000-fold starting from horse serum. Typically 20 litres of serum were processed to yield 15-18mg of electrophoretically pure cholinesterase in the form of an active salt-free dry powder. The method included two stages: fractionation with (NH(4))(2)SO(4) and ion-exchange chromatography. The (NH(4))(2)SO(4) stage included, in principle, the acid (pH3) step of the Strelitz (1944) procedure. The step took advantage of the stabilizing effect that 33%-satd. (NH(4))(2)SO(4) has on cholinesterase activity at pH3 and i...
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