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.
Biochemical and physiological effects of catecholamine administration in the horse.
Research in veterinary science    May 1, 1977   Volume 22, Issue 3 357-360 
Anderson MG, Aitken MM.Adrenaline was given intramuscularly to resting horses. It increased heart rate, sweating, blood levels of lactic dehydrogenase, aldolase, creatine kinase, glucose, lactate, free fatty acids and glycerol. Responses to isoprenaline, to noradenaline and to adrenaline after pretreatment with propranolol indicated that beta receptors were involved in stimulation of tachycardia, sweating, lipolysis and muscle glycogenolysis, and alpha receptors in stimulation of liver glycogenolysis and leakage of intracellular enzymes. The time course and relative magnitude of the effects on different enzymes was ...
The effect of training and detraining on lactate dehydrogenase isoenzymes in the horse.
Biochemical and biophysical research communications    April 25, 1977   Volume 75, Issue 4 863-869 doi: 10.1016/0006-291x(77)91462-0
Guy PS, Snow DH.No abstract available
Tissue distribution and blood levels of gamma-glutamyl transferase in the horse.
Equine veterinary journal    April 1, 1977   Volume 9, Issue 2 100-101 doi: 10.1111/j.2042-3306.1977.tb03995.x
Rico AG, Braun JP, Benard P, El Hassan AA, Cazieux A.In the horse, gamma-glutamyl transferase (GGT) was found to be mainly located in the kidneys, liver and pancreas. As renal lesions are followed by a urinary escape of enzyme, it can be assumed that if there are raised serum enzyme levels then the source will be chiefly from the liver and pancreas. In the blood, GGT can be measured either in plasma or serum. Its mean level in 58 horses was 12 U/L. This level was not affected by moderate dilution or slight haemolysis and its activity was only slightly decreased by storage at--30 degrees C. The relative hepatic specificity of this enzyme and its ...
The activity of purine salvage pathway enzymes in murine and horse models of congenital and acquired dysimmunity.
Developmental and comparative immunology    April 1, 1977   Volume 1, Issue 2 165-173 doi: 10.1016/s0145-305x(77)80009-8
Castles JJ, Gershwin ME, Saito W, Ardans A, Osburn B.Previous studies of human congenital immunodeficiency states and in vitro observations of lymphocyte response to mitogens have implicated two purine salvage pathway enzymes, andenosine deaminase (ADA) and nucleoside phosphorylase (NP), as critical in the normal maturation and/or function of the immune system. Based on this information, ADA and NP activities were examined in a variety of congenital and acquired animal models of dysimmunity. The animals studied herein included: congenitally athymic (nude) mice; congenitally asplenic mice; congenitally athymic-asplenic mice; motheaten mice; New Z...
Isolation and properties of prophospholipase A2 and phospholipase A2 from horse pancreas and horse pancreatic juice.
Biochimica et biophysica acta    March 28, 1977   Volume 491, Issue 1 265-274 doi: 10.1016/0005-2795(77)90062-9
Evenberg A, Meyer H, Verheij HM, de Haas GH.Two phospholipases A2 (EC 3.1.1.4) with different isoelectric points have been isolated from horse pancreas in high yield (880 mg/kg tissue). From pancreatic juice the more acidic species was isolated as the sole phospholipase A2. Upon tryptic activation the zymogens release a hepta- and pentapeptide, respectively from the N-terminal part of the protein giving rise to the formation of one single enzyme with a specific activity higher than that of pancreatic phospholipases A2 from other mammalian species. Horse phospholipase A2 differs from the porcine and bovine enzymes with respect to amino a...
Amino acid sequence of phospholipase A2 from horse pancreas.
The Journal of biological chemistry    February 25, 1977   Volume 252, Issue 4 1189-1196 
Evenberg A, Meyer H, Gaastra W, Verheij HM, De Haas GH.The complete amino acid sequence of phosphlipase A2 (EC 3.1.1.4) from horse pancreas was determined. The protein controls of a single polypeptide chain of 125 amino acids and has a molecular weight of 13,927. The chain is crosslinked by seven disulfide bridges. The sequence was determined by automated Edman degradation of the intact protein and several of the large peptide fragments. Smaller peptides were analyzed by manual Edman degradation. Fragmentation of the peptide chain was accomplished by enzymatic digestion with trypsin, chymotrypsin, and thermolysin. The final overlap was found by di...
Steady state kinetics and binding of eukaryotic cytochromes c with yeast cytochrome c peroxidase.
The Journal of biological chemistry    February 10, 1977   Volume 252, Issue 3 919-926 
Kang CH, Ferguson-Miller S, Margoliash E.1. The steady state kinetics for the oxidation of ferrocytochrome c by yeast cytochrome c peroxidase are biphasic under most conditions. The same biphasic kinetics were observed for yeast iso-1, yeast iso-2, horse, tuna, and cicada cytochromes c. On changing ionic strength, buffer anions, and pH, the apparent Km values for the initial phase (Km1) varied relatively little while the corresponding apparent maximal velocities varied over a much larger range. 2. The highest apparent Vmax1 for horse cytochrome c is attained at relatively low pH (congruent to 6.0) and low ionic strength (congruent to...
Guanidination of horse methemoglobin.
Archives of biochemistry and biophysics    February 1, 1977   Volume 179, Issue 1 322-327 doi: 10.1016/0003-9861(77)90117-5
Sakura JD, Rupley JA.Reaction of horse methemoglobin with O-methylisourea at pH 10.2 results in 95% conversion of lysine residues to homoarginine. Analysis of the chymotryptic peptides showed that no single ϵ-amino group was unreactive. Guanidination decreases the dependence of the sedimentation coefficient on hydrogen ion concentration in the range of pH 8 to 11 and did not affect the dependence on protein concentration at pH 7. These results support the conclusion that the lysine side chains involved in subunit contacts have sufficient freedom to accommodate the small changes in bulk and geometry associated wit...
Serum enzyme and protein concentrations in English shire horses.
The Veterinary record    January 29, 1977   Volume 100, Issue 5 91-92 doi: 10.1136/vr.100.5.91
Blackmore DJ, Kent JE.No abstract available
Purification and characterization of equine herpesvirus-induced DNA.
Virology    January 1, 1977   Volume 76, Issue 1 395-408 doi: 10.1016/0042-6822(77)90311-7
Allen GP, O'Callaghan DJ, Randall CC.Infection of cells with equine herpesvirus type 1 (EHV-1) or type 3 (EHV-3) resulted in the induction of a DNA polymerase activity distinguishable from host cell DNA polymerases by its high salt requirement for maximal activity. By column chromatography on DEAE-cellulose, DNA-cellulose, phosphocellulose, and hydroxyapatite, the EHV-1-induced polymerase was purified 500-fold with 1–2% recovery of total activity from the nuclei of infected hamster livers. The final enzyme preparation was homogeneous as judged by electrophoresis in sodium dodecyl sulfate-polyacrylamide gels. Calculations based ...
Metabolism of biogenic amines in the pulmonary circulation.
Bibliotheca anatomica    January 1, 1977   Issue 16 Pt 2 387-389 
Gillis CN.No abstract available
[Comparative electrophoretic study of the molecular forms of alkaline phosphatase in the leukocytes of agricultural animals].
Veterinarno-meditsinski nauki    January 1, 1977   Volume 14, Issue 3 100-104 
Goranov Kh.The alkaline phosphatase enzyme, isolated by Morton's method from leukocytes of sheep, goats, and pigs gave after agarose elctrophoresis two isoenzyme fractions moving to the positive pole at the sites of the alpha 1- and alpha 2-globulins of the blood serum. In bovine leukocytes, besides these two fractions there was a third one that moved more slowly in the zone of the beta-globulins. In horses the alkaline phosphatase of leukocytes produced a wide band within the zones of the beta-globulins and the albumins. It was established that the proportion between the individual isoenzyme fractions o...
The activity of some nucleolytic enzymes in semen and in the secretion of the male reproductive tract.
Andrologia    January 1, 1977   Volume 9, Issue 1 15-22 doi: 10.1111/j.1439-0272.1977.tb01252.x
Mennella MR, Jones MR.The activity of 5'-nucleotidase (EC 1.3.5), cyclic nucleotide phosphodiesterase (EC 2.1.4.17), non-specific phosphodiesterase (EC 3.1.4.1) and ribonuclease (EC 1.7.7.16)has been investigated in the seminal plasma of whole semen and in the secretions of the seminal vesicle, prostate and epididymis of the bull, boar, ram, stallion, jackass, rabbit and man. Bull seminal plasma showed the highest activity for 5'-nucleotidase, cyclic nucleotide phosphodiesterase and ribonuclease; in contrast, stallion and jackass semen were very poor in these enzymes. Ram, rabbit and boar seminal plasma showed inte...
Rapid heterolysis of indophenyl acetate by a constituent of a preparation of horse serum cholinesterase.
Enzyme    January 1, 1977   Volume 22, Issue 2 130-136 doi: 10.1159/000458777
Hubbard CD, Shoupe TS.A transient phase for the hydrolysis of indophenyl acetate by the commercial preparation of horse serum cholinesterase was observed on a stopped-flow spectrophotometer. It was found that the transient process is a reaction of the ester with a major component of the preparation and is not caused by the serum cholinesterase enzyme. This noncholinesterase component was isolated and the dependence of its concentration and that of the ester upon the transient liberation of the indophenolate ion were determined. Studies with the isolated component and subsequent analyses have led to the tentative id...
Identification of the PR prealbumin proteins in horse serum.
Acta veterinaria Scandinavica    January 1, 1977   Volume 18, Issue 4 458-470 doi: 10.1186/BF03548409
Ek N.The Pr protein, which is one of the major equine acidic prealbumins and which consists of a large number of phenotypes, has been studied with regard to its chemical identity. Serum samples of known Pr phenotype which had been treated with varying amounts of bovine trypsin were subjected to starch gel electrophoresis at pH 4.8. When a certain amount of trypsin was used, the Pr protein was markedly affected, whereas the other acidic prealbumins retained their normal electrophoreitic pattern. Extracts from three different regions of the acidic prealbumin field were tested by the casein precipitat...
Copper and the oxidation of hemoglobin: a comparison of horse and human hemoglobins.
Biochemistry    November 30, 1976   Volume 15, Issue 24 5337-5343 doi: 10.1021/bi00669a021
Rifkind JM, Lauer LD, Chiang SC, Li NC.Oxidation studies of hemoglobin by Cu(II) indicate that for horse hemoglobin, up to a Cu(II)/heme molar ratio of 0.5, all of the Cu(II) added is used to rapidly oxidize the heme. On the other hand, most of the Cu(II) added to human hemoglobin at low Cu(II)/heme molar ratios is unable to oxidize the heme. Only at Cu(II)/heme molar ratios greater than 0.5 does the amount of oxidation per added Cu(II) approach that of horse hemoglobin. At the same time, binding studies indicate that human hemoglobin has an additional binding site involving one copper for every two hemes, which has a higher copper...
The purification and kinetic properties of biophosphoglycerate synthase from horse red blood cells.
Archives of biochemistry and biophysics    November 1, 1976   Volume 177, Issue 1 284-292 doi: 10.1016/0003-9861(76)90438-0
Rose AB, Dube S.No abstract available
[Effect of ATP on carbohydrate metabolism].
Veterinariia    November 1, 1976   Issue 11 99-100 
Alekseev MIu.No abstract available
Pharmacology of procaine in the horse: procaine esterase properties of equine plasma and synovial fluid.
American journal of veterinary research    October 1, 1976   Volume 37, Issue 10 1165-1170 
Tobin T, Blake JW, Sturma L, Arnett S.Procaine added to whole equine blood or diluted plasma was hydrolyzed with half times of approximately 9 and 12 minutes, respectively, at 37 C. This hydrolytic activity was sensitive to heating and physostigmine, but did not affect procainamide. At pharmacologic concentrations of procaine, the rate of the hydrolytic reaction depended directly on the concentrations of plasma or procaine in the system and was less in whole blood than in plasma. These properties are consistent with hydrolysis being due to plasma esterases operating at less than saturating procaine concentrations. These esterases ...
[Study of hydrolysis of aminoalcohol ethers, phenol and choline under the action of horse blood serum cholinesterase].
Biokhimiia (Moscow, Russia)    October 1, 1976   Volume 41, Issue 10 1773-1777 
Kundriutskova LA, Kruglikova RI.Hydrolysis of ethers of saturated and unsaturated alcohols and ethers, e.g. phenol and choline, under the action of horse blood serum cholinesterase, was studied. The reactivity towards enzymatic hydrolysis is decreased due to a greater length of the chain in the alcohol residue of the benzoic acid aminoethers; at nCH2 = 4 the compound is a poor substrate. An increase in nydrophobicity of the acyl residue of the ether molecule also leads to a decrease in the Vmax and Km values. In case of cholinesterase substrates, an increase in the molecule hydrophobicity results in an increase of its non-pr...
Composition and molecular weights of butyrylcholinesterase from horse serum.
Archives of biochemistry and biophysics    September 1, 1976   Volume 176, Issue 1 71-81 doi: 10.1016/0003-9861(76)90142-9
Teng TL, Harpst JA, Lee JC, Zinn A, Carlson DM.No abstract available
Pharmacology of procaine in the horse: a preliminary report.
American journal of veterinary research    September 1, 1976   Volume 37, Issue 9 1107-1110 
Tobin T, Blake JW, Tai CY, Arnett S.Rapid intravenous injection of 1 g of procaine hydrochloride in Thoroughbred mares produced variable signs of central nervous system excitation for as long as 4 minutes. Plasma concentrations of procaine were similarly variable and transient, decreasing with a half-life of approximately 25 minutes. In vitro, plasma from freshly collected equine blood hydrolyzed procaine with a half-life of approximately 7.5 minutes. This hydrolysis was apparently due to plasma esterases. Penicillin, when added free or complexed as procaine-penicillin, did not protect procaine against hydrolysis by these plasma...
Hemagglutination by equine infectious anemia virus.
Infection and immunity    August 1, 1976   Volume 14, Issue 2 325-331 doi: 10.1128/iai.14.2.325-331.1976
Sentsui H, Kono Y.Equine infectious anemia (EIA) virus which was propagated on an equine dermal cell line agglutinated guinea pig erythrocytes. Viral fluids containing about 10(7.5) mean tissue culture infective doses/ml showed hemagglutinating (HA) titers ranging from 16 to 32 units/0.05 ml. Results of cesium chloride equilibrium density gradient centrifugation revealed that the hemagglutinin was inseparable from the virus particles. The hemagglutination reaction persisted over a wide range of temperature and pH, and the absence of divalent cations did not decrease its activity. The HA activity was stable at 4...
Kinetics of the hydrolysis of synthetic substrates by horse urinary kallikrein and trypsin.
General pharmacology    August 1, 1976   Volume 7, Issue 2-3 167-171 doi: 10.1016/0306-3623(76)90056-2
Sampaio MU, Galembeck F, Paiva AC, Prado ES.The kinetic constants for horse urinary kallikrein and trypsin hydrolysis of BAEE, TAME, bradykinin methyl ester and bradykinyl-Ser-Val-Gin-Val-Ser were determined. The values of the ratio kcat/Km show that (1) kallikrein is catalytically less efficient than trypsin for all the substrates (2) the three esters are equally good substrates for trypsin while horse urinary kallikrein is 100-fold more effective on bradykinin methyl ester than on the other substrates (3) for both enzymes the ester of bradykinin is a better substrate than the tetradecapeptide.
Active-site labelling of kallikreins by chloromethylketone derivatives.
General pharmacology    August 1, 1976   Volume 7, Issue 2-3 163-166 doi: 10.1016/0306-3623(76)90055-0
Sampaio CA, Prado ES.Ala-Phe-Lys-CH2-Cl is a chloromethylketone derivative which is able to promote the inhibition of several proteolytic enzymes. In this paper the inhibition of horse urinary and plasmatic kallikreins is described and this inhibition is compared to that produced in human plasma kallikrein. This compound was designed based upon the structure of bradykinin. This enzyme substrate system can provide a model for the study of the interactions between bradykinin and its receptor. The inhibition of the enzymes was achieved both for its esterase and kinin-releasing activities.
Myodegeneration and suspected selenium/vitamin E deficiency in horses.
Journal of the American Veterinary Medical Association    July 15, 1976   Volume 169, Issue 2 213-217 
Wilson TM, Morrison HA, Palmer NC, Finley GG, van Dreumel AA.The clinical, macroscopic, and microscopic features of 10 isolated cases of myodegeneration in foals were compared. Low values for selenium and vitamin E content were found in the hay and oats from one breeding stable. Serum selenium concentrations in mares at this stable were also low. Creatinine phosphokinase and serum glutamic oxaloacetic transaminase activities were increased in 2 young foals at this stable; in 1 of these foals, both enzymatic activities were markedly reduced after treatment with vitamin E and selenium. Nutritional myodegeneration was suggested as a diagnosis in this stabl...
Biochemical studies on equine infectious anaemia.
Folia veterinaria Latina    July 1, 1976   Volume 6, Issue 3 275-288 
Palomba E, Martone F, Meduri A, Vaccaro A, Damiani N.A description is given of an outbreak of equine infectious anaemia (E.I.A.) in Campania [at Naples and Aversa (Caserta)]; it was diagnosed by clinical, pathological and serological examinations (Coggins test). Using the serum of 45 horses with E.I.A. and 11 healthy horses (controls), numerous investigations were carried out on: enzymes, intrinsic coagulation factors, lipids and other substances. The results obtained were very interesting and show that in this disease there are significant increases in many enzymes (LDH, LAP, gamma-GT, CPK, PK and ALD) and copper. Insignificant increases were f...
Crystalline 3-phospho-d-glycerate kinase from horse muscle.
Biochemistry    June 29, 1976   Volume 15, Issue 13 2899-2901 
Johnson PE, Maister SG, Knowles JR.Phosphoglycerate kinase has been isolated in crystalline form from horse muscle. A convenient isolation procedure is described that yields homogeneous enzyme of specific activity 700 units/mg (30 degrees C). The enzyme is monomeric, and has a molecular weight 47 000. Of the eight cysteine residues in the protein, two react rapidly with Nbs21 with the concomitant loss of the catalytic activity. Since the isolation of phosphoglycerate kinase from yeast (Bücher, 1955) there have been several reports of purification methods yielding enzyme approaching molecular homogeneity, from rabbit muscle (Be...
Letter: Kinetics of reduction of horse-heart ferricytochrome c by catechol.
Journal of the American Chemical Society    June 23, 1976   Volume 98, Issue 13 4023-4024 doi: 10.1021/ja00429a061
Toppen DL.No abstract available
The influence of hepatic microsomal amidopyrine demethylase activity on halothane hepatotoxicity in the horse.
The Journal of pathology    June 1, 1976   Volume 119, Issue 2 105-112 doi: 10.1002/path.1711190205
Gopinath G, Ford EJ.The hepatotoxic effect of oral halothane in the horse is increased by pretreatment with phenobarbitone or DDT but not by chlorpromazine. Phenobarbitone and DDT increase the activity of hepatic amidopyrine N-demethylase but chlorpromazine does not. Carbon disulphide protects the liver of the horse against halothane.
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