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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.
Rapid heterolysis of indophenyl acetate by a constituent of a preparation of horse serum cholinesterase. 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. 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. 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...
Pharmacology of procaine in the horse: procaine esterase properties of equine plasma and synovial fluid. 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]. 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...
Pharmacology of procaine in the horse: a preliminary report. 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. 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. 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. 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. 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. 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. 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...
The influence of hepatic microsomal amidopyrine demethylase activity on halothane hepatotoxicity in the horse. 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.
Steady-state enzyme kinetics of the pancreatic ribonucleases from five mannalian species. The kinetic parameters Km, k+2 and k+2/Km of the pancreatic ribonucleases (EC 3.1.4.22) from cow, giraffe, horse, rat and lesser rorqual have been determined, using 2',3'-cyclic cytidine monophosphate and 2',3'-cuclic uridine monophosphate as substrates. No large differences were found between the activities of the five enzymes. The relative differences between the activities of the five enzymes are mainly due to differences in the rates of hydrolysis and not to differences in the affinities for the substrates.
Isolation of kappa-casein-like proteins from milks of various species. Kappa-Casein-like proteins were isolated from the milks of cow, goat, reindeer, horse, rat, and rabbit. When treated with rennin, all of the isolated kappa-casein components yielded para-kappa-casein-like bands on gel electrophoresis. The rate of cleavage of these components with rennin was determined by measuring material soluble in trichloroacetic acid (macropeptide). The curves were characteristic of a limited, specific attack by rennin on these proteins. The goat and reindeer kappa-caseins were nearly as bovine kappa-casein, but the cleavage of horse, rat, and rabbit kappa-casein-like comp...
Horse-liver alcohol dehydrogenase and Pseudomonas testosteroni 3(17)beta-hydroxysteroid dehydrogenase transfer epimeric hydrogens from NADH to 17beta-hydroxy-5alpha-androstan-3-one. An exception to one of the Alworth-Bentley rules. In the reduction of 17beta-hydroxy-5alpha-androstan-3-one to the 3beta-alcohol, horse liver alcohol dehydrogenase utilizes the 4-pro-R hydrogen of NADH whereas the 3(17)beta-hydroxysteroid dehydrogenase of Pseudomonas testosteroni utulized the 4-pro-S hydrogen. These observations provide an exception to the rule proposed by Alworth and Bentley that with regard to the paired methylene hydrogens at C-4 of NADH and NADPH "the stereospecificity of a particular reaction is fixed and does not vary with the source of the enzyme preparation". It is also apparent that for these two enzymes, the selecti...
Characterization of protein phosphokinase activities in horse thyroid nuclei. The distribution of protein phosphokinase (EC 2.7.1.37) activities has been established in horse thyroid nuclei. The presence of several enzyme activities has been demonstrated, two of which are clearly distinct. The first one acts on histone as substrate and is activated by cyclic AMP. Physico-chemical properties of this nuclear cyclic AMP-dependent histone kinase and of the cytosol histone kinase are different, demonstrating the absence of a contamination from the cytosol. The second enzyme acts on casein as substrate and is not stimulated by cyclic AMP POR CYCLIC GMP. The findings are consi...
Inactivation of horse liver alcohol dehydrogenase by modification of cysteine residue 174 with diazonium-1H-tetrazole. Diazonium-1H-tetrazole was tested as a potential active-site-directed reagent for amino acid residues involved in catalysis by alcohol dehydrogenase. In a novel reaction with a protein, diazonium-1H-tetrazole inactivated the enzyme selectively, and almost stoichiometrically, but reacting with the sulfur of a cysteine residue, Cys-174. As a model compound, the tetrazole adduct of free cysteine was prepared. Elementary and spectral analyses of the adduct were consistent with the structure 5-tetrazoleazo-S-cysteine. The adduct absorbs light with a maximun at 316 nm, and is destroyed by irradiatio...
Effects of training on biochemical values in standardbred horses. Effects of training at a regular, fixed, standard exercise load on venous lactic acid, mixed venous and arterial blood gases and pH, and serum muscle enzymes were determined on previously unconditioned, healthy, adult, Standardbred horses. Arterial and mixed venous blood gases, pH, and serum muscle enzymes did not change in a consistent manner during training. Venous lactic acid concentrations did increase significantly with training and may be of value for the biochemical evaluation of fitness in horses.
The effect of exercise on the lactic dehydrogenase and creatine kinase isoenzyme composition of horse serum. The distribution of lactic dehydrogenase, aldolase and creatine kinase in various horse tissues was determined. Using polyacrylamide gel electrophoresis the lactic dehydrogenase and creatine kinase isoenzyme composition of horse serum, taken before and after exercise, was studied. Horse tissue isoenzyme patterns were also obtained. By comparing tissue and serum patterns, skeletal muscle was found to be the tissue of origin of the increase in serum lactic dehydrogenase and creatine kinase observed after exercise.
Plasma bile acid elevation following CCI4 induced liver damage in dogs, sheep, calves and ponies. Plasma bile acid concentration was determined in normal dogs,sheep, calves and ponies for three days before and six days after liver damage, induced by carbon tetrachloride. In all species, a significant increase in plasma bile acid concentration was associated with a concomitant significant increase in plasma sorbitol dehydrogenase and transferase activity. Plasma bilirubin also significantly increased in all animals except the dogs. Results suggested that plasma bile acid levels could be used to test liver function in domestic animals.
Evaluation of adenosine deaminase and other purine salvage pathway enzymes in horses with combined immunodeficiency. Foals with combined immunodeficiency had normal levels of purine salvage pathway enzymes, including adenosine deaminase, nucleoside phosphorylase, and xanthine oxidase.
Isolation and some molecular parameters of elastase-like normal proteinases from horse blood leucocytes. Cytoplasmic granules were isolated from horse blood polymorphonuclear leucocytes by the heparin method and extracted with 0.9% NaCl by repeated freezing. Soluble proteins were separated on a column of Sephadex G-75 followed by chromatography on a column of CM-Sephadex with a NaCl gradient. Gel filtration, density-gradient centrifugation, isoelectric focusing and 0.1% sodium dodecyl sulphate/polyacrylamide-gel electrophoresis at pH 7.0 and at pH 4.5 were used to determine molecular parameters of proteinases. Three enzymes hydrolysing both casein and N-benzyloxycarbonyl-L-alanine nitrophenyl est...
