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.
Substrate specificity and modifications of the active centre of elastase-like neutral proteinases from horse blood leucocytes.
The Biochemical journal    February 1, 1976   Volume 153, Issue 2 397-402 doi: 10.1042/bj1530397
Koj A, Chudzik J, Dubin A.Two proteinases (2A and 2B) purified from the granular fraction of horse blood leucocytes degrade casein (Km values 12.8 and 6mg/ml respectively) with maximum activity at pH 7.4 and in the presence of 2m-urea. Urea-denatured haemoglobin, fibrinogen, albumin and resorcin/fuchsin-stained elastin are digested at a slower rate. The enzymes hydrolyse synthetic substrates of elastase, N-benzyloxycarbonyl-L-alanine 4-nitrophenyl ester (Km 0.114 and 0.178 mM) and N-acetyl-tri-L-alanine methyl ester (Km 5.55 and 0.98 mM), but they do not hydrolyse synthetic substrates of trypsin, chymotrypsin and throm...
Fiber types and size in equine skeletal muscle.
American journal of veterinary research    February 1, 1976   Volume 37, Issue 2 145-148 
Aberle ED, Judge MD, Kirkham WW, Page EH, Crawford BH.Frozen sections of equine musculus semitendinosus were examined for myosin adenosine triphosphatase (ATPase) and reduced nicotinamide adenine dinucleotide-tetrazolium reductase (NADH-TR), using standard histochemical procedures, and the proportions of the various fiber types and average fiber sectional size were determined. With ATPase staining, approximately 70% of the fibers were classified as alpha fibers (ATPase positive), and 30%, as beta fibers (ATPase negative). In addition, 2 populations of alpha fibers could be readily distinguished on the basis of the intensity of the ATPase reaction...
Characterization of human, bovine, and horse antithrombin III.
Biochemistry    January 27, 1976   Volume 15, Issue 2 368-373 doi: 10.1021/bi00647a020
Kurachi K, Schmer G, Hermodson MA, Teller DC, Davie EW.A comparison of the physical-chemical properties of human, bovine, and horse antithrombin III has been made. These three plasma proteins are strong inhibitors of bovine factor Xa and form a 1:1 molar complex with this coagulation enzyme. Human, bovine, and horse antithrombin III are glycoproteins containing hexose, hexosamine, and neuraminic acid. The total carbohydrate was 9, 12, and 16% for human, bovine, and horse antithrombin III, respectively. These proteins have a similar amino acid composition, although some monor variations were noted. Each antithrombin III is composed of a single poly...
Chemical modification as a probe of the topography and reactivity of horse-spleen apoferritin.
European journal of biochemistry    January 15, 1976   Volume 61, Issue 2 545-550 doi: 10.1111/j.1432-1033.1976.tb10049.x
Wetz K, Crichton RR.In apoferritin, but not in ferritin, 1.0 +/- 0.1 cysteine residue per subunit can be modified. In ferritin 3.3 +/- 0.3 lysine residues and 7.1 +/- 0.7 carboxyl groups per subunit can be modified, whilst the corresponding values for apoferritin are 4.4 +/- 0.4 lysine residues and 11.0 +/- 0.4 carboxyl groups per subunit. Modification of lysine residues which maleic anhydride and carboxyl groups with glycineamide in apoferritin which has been dissociated and denatured in guanidine hydrochloride leads to the introduction of 9.1 +/- 0.5 maleyl groups per subunit and 22.0 +/- 0.9 glycineamide resid...
[Equine pepsins].
Biokhimiia (Moscow, Russia)    January 1, 1976   Volume 41, Issue 7 1285-1290 
Stepanov VM, Lavrenova GI, Rudenskaia GN, Gonchar MV, Lebareva LS.6 forms of pepsin are found in horse gastric juice. Amino acid sequence is determined of N-terminal (most variable) part of polypeptide chain of main pepsin components. Equine pepsines, which have pI 2.1 and 2.3, are found to have identical amino acid sequence at least for 31 amino acid residues. The same sequence is observed in the component with pI 2.6 for 10 first residues. The sequence of equine pepsin with pI 3.2 has 3 substitutions for 33 amino acids, when compared with pepsines having pI 2.1 and 2.3. The forms of equine pepsin studied are more similar than the other isoenzyme pair, huma...
Creatine phosphokinase in normal sheep and in sheep with nutritional muscular dystrophy.
Journal of comparative pathology    January 1, 1976   Volume 86, Issue 1 23-28 doi: 10.1016/0021-9975(76)90023-2
Boyd JW.No abstract available
Acid phosphatase heterogeneity in horse neutrophil and eosinophil leukocytes.
Enzyme    January 1, 1976   Volume 21, Issue 6 540-552 doi: 10.1159/000458906
Heyneman RA, Bruyninckx WJ, Vercauteren RE.Two distinct groups of acid phosphatase containing granules were characterized in neutrophils, each group displaying different multiple forms of the enzyme. The heavy granule acid phosphatase showed a lysosomal location. A second lighter group of particles contained a thermolabile, thiol-dependent acid p-nitrophenyl and alpha-naphtylphosphatase, an enzyme clearly different from lysosomal acid phosphatase. Acid phosphatase activity from eosinophil leukocytes appeared to be totally associated with the typical eosinophil granules. On mechanical disruption of these particles, an acid phosphatase w...
LDH and LDH isoenzymes of synovial fluid in the horse.
Acta veterinaria Scandinavica    January 1, 1976   Volume 17, Issue 2 178-189 doi: 10.1186/BF03547926
Rejnö S.LDH is an intracellular enzyme, which when cells degenerate is released to the extracellular spaces and body fluids. Cells and organs in the mammalian body differ from each other with respect to their LDH isoenzyme patterns. These circumstances have led to the use of LDH isoenzyme determinations in laboratory diagnostic work. In the present investigation total LDH activity and LDH isoenzyme distribution in equine synovial fluid from healthy joints, joints with serous arthritis, osteochondrosis dissecans and arthrosis, were determined. The fluids from the diseased joints differed from normal sy...
[Studies on the activity, properties and isoenzymes of acid phosphatase in the erythrocytes of swine, horse, dog, cat, duck and chicken].
Archiv fur experimentelle Veterinarmedizin    January 1, 1976   Volume 30, Issue 4 585-597 
Zobel G, Kolb FE.Acid phosphatase of erythrocytes of several species was investigated, with three isozymes having been recorded from swine (three types), three (two types) from horse, four (one type) from dog, two (two types) from cat, two (three types) from duck, and two (one type) from fowl. The Michaelis constant of the enzyme varied between 3.5 and 5 X 10(-4) M for the species involved. The species, however, differed slightly for the optimum pH of the enzyme. The average enzymatic activities were (5.68 +/- 0.42 for dog, 4.46 +/- 1.0 for horse, 3.8 +/- 0.24 for swine, 3.72 for cat, 2.5 +/- 0.62 for duck, an...
N-acetylserine in horse muscle acylphosphatase.
International journal of peptide and protein research    January 1, 1976   Volume 8, Issue 3 269-273 
Cappugi G, Chellini PC, Nassi P, Ramponi G.A ninhydrin-negative peptide fraction obtained from tryptic digest of carboxymethyl acylphosphatase was isolated by chromatography on a column of PA 28 Beckman resin and analysed for the amino acid composition. Degradation with carboxypeptidase B and A indicated that the sequence of this peptide was: X-Thr-Ala-Arg. The amino-terminal residue was identified as N-acetylserine by high voltage electrophoresis. It is therefore suggested that the sequence of the NH2-terminal portion of CM-acylphosphatase is N-acetyl-Ser-Thr-Ala-Arg. Digestion with carboxypeptidase A and B indicated also that the COO...
Erythrocyte enzyme activities and glutathione levels of the horse, cat, dog and man.
Comparative biochemistry and physiology. B, Comparative biochemistry    December 15, 1975   Volume 52, Issue 4 507-510 doi: 10.1016/0305-0491(75)90226-6
Harvey JW, Kaneko JJ.No abstract available
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
1 51 52 53 54 55 61