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.
The catalytic metal atoms of cobalt substituted liver alcohol dehydrogenase.
Biochemical and biophysical research communications    December 15, 1975   Volume 67, Issue 4 1488-1493 doi: 10.1016/0006-291x(75)90194-1
Sytkowski AJ, Vallee BL.The catalytic and non-catalytic Zn atom pairs of horse liver alcohol dehydrogenase (LADH) have been replaced sequentially either by 65Zn, Co or 65Zn and Co. The Co derivatives exhibit characteristic spectra. When Co replaces the Zn atoms which exchange secondly, enzymatic activity is altered, and both imidazole and 1,10-phenanthroline (OP) significantly modify the spectrum of the catalytic Co atoms. Further, due to the removal of cobalt, the instantaneous and reversible OP inhibition of the native enzyme becomes time-dependent and irreversible. Jointly, these data identify the pair of metal at...
[Estimation of the concentration of urea in the blood of horses, cattle, goats and dogs using the “Merckognost Harnstoff” method compared with an enzymatic, photometric method (author’s transl)].
Tijdschrift voor diergeneeskunde    November 1, 1975   Volume 100, Issue 21 1137-1142 
Schotman AJ, Wensing T, Ockels J, de Bruyne JJ, Hendriks HJ.To examine the suitability and reliability in field use of the "Merckognost Harnstoff" method in estimating the concentration of urea in the blood of horses, cattle, goats and dogs, the levels determined by this procedure were compared with those determined by an enzymatic (urease) photometric method widely used in laboratories. It was concluded from the results obtained that estimation using the "Merckognost Harnstoff" is sufficiently reliable for the rapid assay of urea in the blood under field conditions.
The development and distribution of mucosal enzymes in the small intestine of the fetus and young foal.
Journal of reproduction and fertility. Supplement    October 1, 1975   Issue 23 717-723 
Roberts MC.Lactase and cellobiase were detectable in the fetal intestine by the 3rd month of gestation, and although there was little change by the 9th month, maximal levels were reached at birth and steadily declined after 4 months. Conversely maltase, sucrase and trehalase were barely discernible in the fetus, maltase being present at low levels at birth, but all increased during the suckling period to attain adult levels by 7 months of age. Alkaline phosphatase activity matured earlier than did disaccharidase activity. Mucosal enzymes other than alkaline phosphatase were virtually absent from meconium...
Carbonic anhydrase isozymes in American ponies and riding horses: a new polymorphic high-activity type isozyme.
Biochemical genetics    October 1, 1975   Volume 13, Issue 9-10 643-649 doi: 10.1007/BF00484922
Deutsch HF, Bray RP.A study of the erythrocyte carbonic anhydrases of 219 American ponies and 76 riding horses has revealed the presence of five variants of the low-activity CA B isozyme and two variants of the high-activity CA C isozyme. The previously undetected variant of CA C was found only in the pony population and had an allele frequency of 8.9%. A family study of animals possessing the CA B variant A2 showed an unexpected high frequency of inheritance.
The distribution of delta5-3beta-hydroxysteroid dehydrogenase in the graafian follicle of the mare.
Journal of reproduction and fertility. Supplement    October 1, 1975   Issue 23 323-327 
Hay MF, Allen WR, Lewis IM.Graafian follicles of various sizes obtained from mares at different stages of the oestrous cycle were examined histologically and histochemically for delta5-3beta-hydroxysteroid dehydrogenase (3beta-HSD) activity and related enzymes. The 3beta-HSD activity was not found in the theca interna of any follicles but was present in the membrana granulosa of well-vascularized large follicles in the late luteal phase of the cycle and at oestrus. These findings indicate that pregnenolone cannot be converted into progesterone in the theca interna. It is suggested that this conversion occurs in the memb...
A histochemical study of steroid metabolism in the equine fetus and placenta.
Journal of reproduction and fertility. Supplement    October 1, 1975   Issue 23 569-573 
Flood PF, Marrable AW.The distribution of several hydroxysteroid dehydrogenases (HSD) was examined in a variety of equine placental and fetal tissues. The main points of interest were: (a) the lack of dehydrogenase activity in the gonad, (b) the appearance of a variety of HSDs in the trophoblast as early as 13 days of gestation, (c) the histochemical similarity between the cells of the trophoblast and the endometrial cup, and (d) the restriction of the strong endometrial 17beta-HSD reaction to those parts of the uterine epithelium directly apposed to the trophoblast.
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...
Digitoxin metabolism by rat liver microsomes.
Biochemical pharmacology    September 1, 1975   Volume 24, Issue 17 1639-1641 doi: 10.1016/b978-0-12-152810-2.50012-7
Schmoldt A, Benthe HF, Haberland G, Scott WA, Mahoney E, BOSE SK.No abstract available
Digitoxin metabolism by rat liver microsomes.
Biochemical pharmacology    September 1, 1975   Volume 24, Issue 17 1639-1641 
Schmoldt A, Benthe HF, Haberland G.No abstract available
Digitoxin metabolism by rat liver microsomes.
Biochemical pharmacology    September 1, 1975   Volume 24, Issue 17 1639-1641 doi: 10.1016/b978-0-12-152810-2.50012-7
Schmoldt A, Benthe HF, Haberland G, Scott WA, Mahoney E, FISCHER H, FELDT K.No abstract available
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...
Digitoxin metabolism by rat liver microsomes.
Biochemical pharmacology    September 1, 1975   Volume 24, Issue 17 1639-1641 doi: 10.1016/0005-7967(77)90095-x
Schmoldt A, Benthe HF, Haberland G, Sinelnikova EM, Dvoretskova TV, Kagan ZS, Marshall WL, Stoian M, Andrews WR.It has been shown that for the reaction catalyzed by "biodegradative" L-threonine dehydratase from E. coli strains K-12 and 980 in 0.5 M phosphate-carbonate buffer, pH 8.4 and pH 9.5, the plots of initial reaction rate (v) versus the initial substrate concentration ([S]0 are characterized by several inflection points, i. e. an intermediate plateau. The plot of v versus the allosteric activator (AMP) concentration have very complicated shapes: there are several inflection points, and also the maximum at L-threonine concentration equal to 3-10(2) and 5-10(-2) M. High AMP concentrations inhibit t...
Digitoxin metabolism by rat liver microsomes.
Biochemical pharmacology    September 1, 1975   Volume 24, Issue 17 1639-1641 doi: 10.1016/0006-291x(75)90200-4
Schmoldt A, Benthe HF, Haberland G, Jallon JM, Risler Y, Iwatsubo M, Karuzina II, Bachmanova GI, Kuznetsova GP, Izotov MV, Archakov AI, Kröger H....It has been found that NADPH-dependent hydroxylation of dimethylaniline, aniline, p- and o-nitroanisol and lipid peroxidation is inhibited by the tyrosine-copper (II) complex (low molecular weight analog of superoxide dismutase), which is indicative of a possibility of superoxide radicals formation in these reactions. The inhibition of the above-mentioned reactions with Tyr2-Cu2+ is less pronounced or absent, if cumole hydroperoxide is used as cosubstrate instead of NADPH. Differences in the Tyr2-Cu2+ complex effects on the cumule hydroperoxide-dependent xenobiotics hydroxylation and lipid per...
[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...
1 51 52 53 54 55 61