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.
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...
Influence of acepromazine/etorphine and azaperone/metomidate on serum enzyme activities on the horse.
Research in veterinary science    November 1, 1974   Volume 17, Issue 3 395-397 
Hillidge CJ, Lees P, Mullen PA, Serrano L.No abstract available
Amylase activity in the small intestine of the horse.
Research in veterinary science    November 1, 1974   Volume 17, Issue 3 400-401 
Roberts MC.No abstract available
Proceedings: Influence of pressure on the reduction of horse heart ferricytochrome c with potassium ferrocyanide.
Archives internationales de physiologie et de biochimie    October 1, 1974   Volume 82, Issue 4 792 
Vandersypen HA, Heremans KA.No abstract available
[The occurrence of glutamic-oxaloacetic transaminase in stallion semen and its relationship to other properties of the semen].
Zuchthygiene    September 1, 1974   Volume 9, Issue 3 129-136 
Hillmann KH, Treu H.No abstract available
A steady-state kinetic model of butyrylcholinesterase from horse plasma.
The Biochemical journal    September 1, 1974   Volume 141, Issue 3 825-834 doi: 10.1042/bj1410825
Augustinsson KB, Bartfai T, Mannervik B.The steady-state kinetics of the butyrylcholinesterase-catalysed hydrolysis of butyrylthiocholine and thiophenyl acetate were shown to deviate from Michaelis-Menten kinetics. The ;best' empirical rate law was selected by fitting different rate equations to the experimental data by non-linear regression methods. The results were analysed in view of two alternative interpretations: (1) the reaction is catalysed by a mixture of enzymes, or (2) the activity is due to a single enzyme displaying deviations from Michaelis-Menten kinetics. It was concluded that the second alternative applies, and this...
Horse pancreatic ribonuclease.
European journal of biochemistry    July 15, 1974   Volume 46, Issue 2 221-233 doi: 10.1111/j.1432-1033.1974.tb03615.x
Scheffer AJ, Beintema JJ.No abstract available
Organophosphate splitting serum enzymes in different mammals.
Comparative biochemistry and physiology. B, Comparative biochemistry    July 15, 1974   Volume 48, Issue 3 427-433 doi: 10.1016/0305-0491(74)90277-6
Zech R, Zürcher K.No abstract available
The development and distribution of small intestinal disaccharidases in the horse.
Research in veterinary science    July 1, 1974   Volume 17, Issue 1 42-48 
Roberts MC, Hill FW, Kidder DE.No abstract available
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