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.
Seasonal changes in blood serum protein fractions and in activity of AspAT and AlAT in Arabian brood mares and their foals.
Comparative biochemistry and physiology. A, Comparative physiology    January 1, 1985   Volume 82, Issue 1 167-178 doi: 10.1016/0300-9629(85)90722-4
Gill J, Jakubów K, Kompanowska-Jezierska E, Kott A, Szumska D.In 34 pure breed Arabian horses divided into four groups (Gr. I--10 pregnant mares, Gr. II--7 barren mares, Gr. III--10 foals born in 1981, Gr. IV--7 foals born in 1982) seasonal changes in total blood serum protein, its electrophoretic fractions and the activity of AspAT and AlAT were studied. Seasonal cyclicity was found in all groups in the amount of total serum proteins, and alpha 2- and beta 1-globulin fractions. Cyclicity was found in the level of albumin and activity of AspAT in three groups, not Gr. II, and in gamma-globulin, not Gr. IV. beta 2-globulin and AlAT cyclicity was found in ...
Horse leucocyte proteinase-inhibitor system. Kinetic parameters of the inhibition reaction.
The International journal of biochemistry    January 1, 1985   Volume 17, Issue 4 509-513 doi: 10.1016/0020-711x(85)90147-8
Dubin A, Potempa J, Silberring J.Horse leucocyte neutral proteinase inhibitor reacts with all tested elastases at the molar ratios of 1:1 and yielding stable complexes (Ki = 10(-10) M). The above reactions are very rapid, characterized by the high values of association rate constant kon = 10(7) M-1s-1.
Metabolic investigations of fibroblasts from horses, Equus caballus, with hereditary severe combined immunodeficiency.
Comparative biochemistry and physiology. B, Comparative biochemistry    January 1, 1985   Volume 81, Issue 3 781-786 doi: 10.1016/0305-0491(85)90405-5
Magnuson NS, Perryman LE, Suttle DP, Robinson JL, Mason PH, Marta KM.In an attempt to determine the metabolic defect causing severe combined immunodeficiency (SCID) in horses in which altered purine metabolism has been observed, various parameters of purine and pyrimidine metabolism were evaluated. The activities of nine purine enzymes (adenosine kinase, purine nucleoside phosphorylase, deoxyadenosine kinase, deoxycytidine kinase, 5'-nucleotidase, AMP deaminase, hypoxanthine-guanine phosphoribosyl transferase, and adenine phosphoribosyl transferase were measured in fibroblasts. All activities determined for SCID horses were normal. Uptake of 10 microM adenosine...
Evaluation of a technique for measurement of gamma-glutamyltranspeptidase in equine urine.
American journal of veterinary research    January 1, 1985   Volume 46, Issue 1 147-150 
Adams R, McClure JJ, Gossett KA, Koonce KL, Ezigbo C.gamma-Glutamyltranspeptidase (GGT) activity in equine urine was measured, using an assay developed for use with serum and was found to be reproducible. The GGT activity was measured in samples prepared by serial dilution of exogenous GGT with equine urine, and the activity was determined to be linear between 21 IU/L and 407 IU/L. The behavior of exogenously added GGT was compared in equine serum and urine. The enzyme behaved similarly in both fluids. The GGT activity was measured in serum and urine samples after storage at -20, 4, and 25 C for 24 and/or 72 hours. Enzyme activity decreased afte...
Comparison of fiber types in skeletal muscles from ten animal species based on sensitivity of the myofibrillar actomyosin ATPase to acid or copper.
Histochemistry    January 1, 1985   Volume 82, Issue 2 175-183 doi: 10.1007/BF00708203
Matoba H, Allen JR, Bayly WM, Oakley CR, Gollnick PD.Comparisons were made of the histochemical characteristics of skeletal muscle from 10 animal species. The basic comparison was made from the staining patterns for the myofibrillar actomyosin ATPase produced by preincubation of fresh frozen cross-sections of muscle at alkaline pH (10.30) or acid pH (4.60) with those produced by preincubation in media containing Cu2+ at alkaline pH (10.30), near neutral pH (7.40), or acid pH (4.60). Muscle sections were also stained for reduced nicotinamide adenine dinucleotide tetrazolium reductase and alpha-glycerophosphate dehydrogenase to provide an indicati...
Neutrophilic leukocyte structure and function in domestic animals.
Advances in veterinary science and comparative medicine    January 1, 1985   Volume 30 91-129 
Bertram TA.Differences in neutrophil morphology between various species of domestic animals are evident when morphometric techniques are used. Morphometric analysis can be coupled with functional assays of degranulation to demonstrate changes in granule volume after neutrophil activation (Bertram and Jensen, 1984). Morphometric and functional analysis of the neutrophil can also be used to evaluate the response of neutrophils to infectious agents (Coignoul et al., 1984a). Comparison of these assays between animal species may provide insight into the susceptibility of animals to various microbial pathogens...
Microquantitative determination of the distribution patterns of alcohol dehydrogenase activity in the liver of rat, guinea-pig and horse.
Histochemistry    January 1, 1985   Volume 83, Issue 5 431-436 doi: 10.1007/BF00509205
Maly IP, Sasse D.Microquantitative measurements of ADH-activity were carried out on the livers of male and female rats, guinea-pigs and horses (two geldings and a mare). Lyophilized cryostat sections of liver parenchyma were microdissected the whole way along the sinusoidal length from the terminal afferent vessels to the terminal efferent venule. ADH activity in samples of about 50-150 ng was measured in a microbiochemical assay using the oil-well technique without enzymatic cycling, by direct luminometric determination of NADH. On the basis of the single measurements, mean values of total hepatic ADH activit...
Unfolding-refolding transition of a hinge bending enzyme: horse muscle phosphoglycerate kinase induced by guanidine hydrochloride.
Biochemistry    December 18, 1984   Volume 23, Issue 26 6654-6661 doi: 10.1021/bi00321a057
Betton JM, Desmadril M, Mitraki A, Yon JM.The unfolding-refolding transition of horse muscle phosphoglycerate kinase induced by guanidine hydrochloride was studied under equilibrium conditions using four different signals: fluorescence intensity at 336 nm, UV difference absorbance at 286 and 292 nm, ellipticity at 220 nm, and enzyme activity. From the following arguments, we found that the process deviates from a two-state model and intermediates are significantly populated even at equilibrium: (1) the noncoincidence of the transition curves and (2) the asymmetry of the transition curve obtained from CD measurements. From these differ...
Antibodies to equine antithymocyte globulin in heart transplant recipients: evaluation of an enzyme immunoassay.
Journal of clinical & laboratory immunology    December 1, 1984   Volume 15, Issue 4 175-180 
Harkiss GD.An isotype-specific microELISA is presented for the measurement of antibodies to equine antithymocyte globulin in human heart transplant recipients. The assay conditions were optimized and evaluated in serial samples from 40 patients receiving a cardiac allograft. The results demonstrate that despite steroid immunosuppression and T cell cytopenia the majority of patients receiving antithymocyte globulin develop significant antibody responses, with some producing very high titres. IgM and IgG isotypes tended to predominate, with peak antibody responses occurring during the second and third week...
Substrate-dependent kinetic behavior of horse plasma cholinesterase: evidence for kinetically distinct populations of active sites.
Archives of biochemistry and biophysics    December 1, 1984   Volume 235, Issue 2 650-656 doi: 10.1016/0003-9861(84)90240-6
Söylemez Z, Ozer I.The inhibition of horse plasma cholinesterase by propranolol showed characteristics which depended upon the identity of the substrate used. With butyrylthiocholine as substrate, the inhibition showed a first-order dependence on inhibitor concentration, and was characterized by a Ki of 8 microM (pH 7.4, 20 degrees C). With p-nitrophenylbutyrate as substrate, a biphasic v-1 versus [I] relationship was obtained. The biphasic curve could be resolved into two components, with apparent Ki's of 9 microM and 1.3 mM. Use of butyrylthiocholine as alternative substrate resulted in partial inhibition of p...
Enzymatic determination of unconjugated oestrogens in faeces for pregnancy diagnosis in mares.
Equine veterinary journal    November 1, 1984   Volume 16, Issue 6 537-539 doi: 10.1111/j.2042-3306.1984.tb02012.x
Bamberg E, Choi HS, Möstl E, Wurm W, Lorin D, Arbeiter K.No abstract available
Isolation and partial characterization of bovine and equine factor D.
Molecular immunology    October 1, 1984   Volume 21, Issue 10 869-876 doi: 10.1016/0161-5890(84)90141-x
Blanchard DB, Leid RW.Bovine and equine factor D were purified to apparent homogeneity as evidenced by a single protein staining band on 7.5-17.5% SDS-PAGE slab gels under both reducing and non-reducing conditions. An apparent mol. wt of 15,000 for bovine D and 22,500 for equine D were noted after SDS-PAGE gel analysis of both reduced and non-reduced preparations. A single polypeptide chain for both proteins was evidenced by the lack of any change in the electrophoretic mobility under each of these conditions. The bovine and equine D were enriched 3347- and 9447-fold, with a 20 and 29% yield of hemolytic activity, ...
[Interaction of bis-phosphorylated methanes with mammalian esterases].
Bioorganicheskaia khimiia    October 1, 1984   Volume 10, Issue 10 1347-1352 
Makhaeva GF, Shataeva GA, Iankovskaia VL, Fetisov VI, Loshadkin NA.The interaction of human erythrocyte acetylcholinesterase, horse serum butyrylcholinesterase and rat liver carboxylesterase with insecticides (RO)2P(O)SCH(COOEt)SP(O)(OR)2 (I) and (RO)2P(O)SCH(COOEt)OP(S)(OR)2 (II) was studied. The type I and II compounds were not hydrolyzed by carboxylesterase and inhibited the esterases irreversibly. A complex pattern of inhibition of acetylcholinesterase and butyrylcholinesterase by these compounds was caused by kinetically-manifested formation of an enzyme-inhibitor complex. The compounds I and II were more selective towards butyrylcholinesterase than towa...
Diamine oxidase from horse kidney: ionic strength dependence of stability and activity.
The Italian journal of biochemistry    September 1, 1984   Volume 33, Issue 5 303-310 
Corda M, Pellegrini M, Rinaldi A.Diamine oxidase was prepared from horse kidney by a procedure involving heat denaturation at 50 degrees C, ammonium sulfate fractionation, chromatography on hydroxyapatite and on G-200 Sephadex columns. This procedure gave about 1000 fold purification over the crude kidney cortex homogenate. The enzyme preparations thus obtained are stable only at high ionic strength. The effect on enzyme activity of salt concentration and various stabilizing agents have been investigated. The horse kidney diamine oxidase is irreversibly inhibited by carbonyl reagents and shows substrate specificity quite simi...
Partial amino-acid sequence and cysteine reactivities of cytosolic aspartate aminotransferase from horse heart.
Biochimica et biophysica acta    August 28, 1984   Volume 789, Issue 1 51-56 doi: 10.1016/0167-4838(84)90059-1
Martini F, Angelaccio S, Barra D, Doonan S, Bossa F.Cytosolic aspartate aminotransferase (L-aspartate:2-oxoglutarate aminotransferase, EC 2.6.1.1) from horse heart has five cysteine residues, two of which can be titrated with 5,5'-dithiobis(2-nitrobenzoid acid) in the native enzyme with no impairment of catalytic activity. The rate of modification is unaffected by the presence of substrates. Reaction with N-ethylmaleimide leads to loss of catalytic activity, the rate of inactivation being increased by the presence of substrates. Peptides containing 361 amino-acid residues (about 88% of the total number in the protein) have been isolated and ali...
Microheterogeneity of type II cAMP-dependent protein kinase in various mammalian species and tissues.
The Journal of biological chemistry    August 25, 1984   Volume 259, Issue 16 10596-10605 
Robinson-Steiner AM, Beebe SJ, Rannels SR, Corbin JD.Excluding autophosphorylated species, at least six forms of the regulatory subunit of type II cAMP-dependent protein kinase (RII) from various mammalian tissues were identified by sodium dodecyl sulfate (SDS) gel electrophoresis of purified samples and of crude preparations photoaffinity labeled with 8-azido[32P] cAMP and by gel filtration. After autophosphorylation some heart RII forms termed type IIA (bovine, porcine, equine, and dog) shifted to a more slowly migrating band on SDS gels while others termed type IIB (rat, guinea pig, rabbit, and monkey) did not detectably shift. Both subclasse...
Kinetics of electron transfer between mitochondrial cytochrome c and iron hexacyanides.
Journal of inorganic biochemistry    August 1, 1984   Volume 21, Issue 4 295-310 doi: 10.1016/0162-0134(84)85052-7
Eley CG, Ragg E, Moore GR.The reduction of horse and Candida krusei cytochromes c by ferrocyanide has been studied by 1H NMR spectroscopy and the reaction found to involve a precursor complex of ferrocyanide bound to ferricytochrome c (pH* 7.4, 2H2O, I = 0.12, and 25 degrees C). The electron transfer rate constants for the reduction of the two ferricytochromes by associated ferrocyanide were found to be the same at 780 +/- 80 sec-1 but the association constants for binding of ferrocyanide to ferricytochrome c were significantly different: horse, 90 +/- 20 M-1 and Candida, 285 +/- 30 M-1. The different association const...
Ascorbate reduction of horse heart cytochrome c. A zero-energy reduction reaction.
The Journal of biological chemistry    July 10, 1984   Volume 259, Issue 13 8144-8150 
Myer YP, Kumar S.The ascorbate reduction of horse heart ferricytochrome c in 0.05 M phosphate + 0.25 M sodium sulfate, at pH 7.3, as a function of temperature, 12-36 degrees C, and at alkaline pH 8.4 using stopped flow technique has been examined. The data have been analyzed in terms of a two-step mechanism, binding followed by reduction (Myer, Y.P., Thallam, K.K., and Pande, A. (1980) J. Biol. Chem. 255, 9666-9673). At neutral pH and up to about 26 degrees C, the first order reduction constant is independent of temperature, i.e. with zero or near-zero activation energy. At higher temperatures, it becomes temp...
[Multiple forms of horse pepsin].
Biokhimiia (Moscow, Russia)    June 1, 1984   Volume 49, Issue 6 1026-1037 
Gonchar MV, Lavrenova GI, Rudenskaia GN, Gaĭda AV, Stepanov VM.Using ion-exchange and affinity chromatography and isoelectrofocusing, eight forms of pepsin with pI 1.6, 1.8, 2.1, 2.3, 2.6, 2.8, 3.2 and 3.6, were isolated from horse gastric juice. The molecular weights, amino acid composition, N-terminal sequence and functional activity of these multiple forms were determined. Partial primary structure of tryptic peptides of pepsin with pI 2.3 was investigated. The analyzed partial sequences of the forms with pI 1.8, 2.1, 2.3, and 2.6 have identical structures which differ from the amino acid sequence of pepsin with pI 3.2 by four substituents. In terms of...
Effect of electromyography on serum creatine kinase values in clinically normal dogs and horses.
American journal of veterinary research    June 1, 1984   Volume 45, Issue 6 1199-1200 
Steiss JE, Forsyth G.The effect of needle electromyography (EMG) on serum creatine kinase (CK) activity was determined, using clinically normal dogs (males and females; n = 8) and horses (females; n = 8). All animals appeared normal on EMG evaluation. Serum CK was measured before and 4, 24, and 48 hours after EMG. Except for a single 24-hour sample in a dog, the animals did not have abnormally increased serum CK activity after EMG. For dogs and horses, mean values were increased, but within normal range at 4 and 24 hours and returned to base-line values by 48 hours after EMG. For dogs, but not for horses, these CK...
Kinetic study of CO and O2 binding to horse heart myoglobin reconstituted with synthetic hemes lacking methyl and vinyl side chains.
Archives of biochemistry and biophysics    June 1, 1984   Volume 231, Issue 2 366-371 doi: 10.1016/0003-9861(84)90399-0
Chang CK, Ward B, Ebina S.Carbon monoxide- and oxygen-binding rates and affinities were measured for horse heart myoglobins reconstituted with synthetic hemes lacking peripheral methyl and vinyl groups. There is an apparent correlation between heme size and ligand specificity, i.e. larger m values (ratios of CO vs O2 association rates, l'/k') with smaller hemes. However, this correlation broke down with the most dealkylated heme. This is interpreted as resulting from protein conformational changes altering the steric crowdedness at the O2-binding site. Spectral properties and autoxidation rates also corroborate this vi...
Preliminary X-ray investigation of enzyme substrate complexes of horse muscle phosphoglycerate kinase.
Journal of molecular biology    May 15, 1984   Volume 175, Issue 2 219-223 doi: 10.1016/0022-2836(84)90476-5
Rice DW, Blake CC.Crystals of horse muscle 3-phosphoglycerate kinase have been grown in the presence of a wide variety of substrates using either potassium tartrate or polyethylene glycol as a precipitant. In those grown from polyethylene glycol, two related crystal forms have been obtained by varying the nature of the substrates present in the crystallization medium. In order to obtain one of these forms, form B, the presence of the substrate 3-phosphoglycerate appears to be essential. The two crystal forms are not interconvertible by simple diffusion experiments and the crystals grown in the absence of 3-phos...
Experimental ischaemia of the ileum and concentrations of the intestinal isoenzyme of alkaline phosphatase in plasma and peritoneal fluid.
Equine veterinary journal    May 1, 1984   Volume 16, Issue 3 215-217 doi: 10.1111/j.2042-3306.1984.tb01909.x
Davies JV, Gerring EL, Goodburn R, Manderville P.No abstract available
Fibre types, enzyme activities and substrate utilisation in skeletal muscles of horses competing in endurance rides.
Equine veterinary journal    May 1, 1984   Volume 16, Issue 3 197-202 doi: 10.1111/j.2042-3306.1984.tb01903.x
Essén-Gustavsson B, Karlström K, Lindholm A.Venous blood samples and middle gluteal muscle biopsies were obtained from 21 horses taking part in 100 km or 50 km endurance rides. Group A consisted of seven horses competing over 100 km (four horses completed the ride). Group B consisted of the six horses that were among the 10 best over 50 km while the other eight horses of Group C completed 50 km at a slower speed. Blood lactate, glycerol and creatine kinase increased in all groups while aspartate aminotransferase levels were higher only in Group A. No changes was found in blood glucose in Groups B and C while horses in Group A had lower ...
The acute inflammatory process, arachidonic acid metabolism and the mode of action of anti-inflammatory drugs.
Equine veterinary journal    May 1, 1984   Volume 16, Issue 3 163-175 doi: 10.1111/j.2042-3306.1984.tb01893.x
Higgins AJ, Lees P.Arachidonic acid is a polyunsaturated fatty acid covalently bound in esterified form in the cell membranes of most body cells. Following irritation or injury, arachidonic acid is released and oxygenated by enzyme systems leading to the formation of an important group of inflammatory mediators, the eicosanoids. It is now recognised that eicosanoid release is fundamental to the inflammatory process. For example, the prostaglandins and other prostanoids, products of the cyclooxygenase enzyme pathway, have potent inflammatory properties and prostaglandin E2 is readily detectable in equine acute in...
Seasonal enzyme activity changes in two aminotransferases AspAT and AlAT, acid and alkaline phosphatases and aldolase in the serum of Thoroughbred horses during a racing season.
Acta physiologica Polonica    May 1, 1984   Volume 35, Issue 3 249-256 
Szwarocka-Priebe T, Gill J.Twenty Thoroughbred 3 year old horses (10 stallions and 10 mares), trained and raced at the Warsaw Race-Course were studied from March through November. Blood was taken approximately every 8 weeks to determine the activities of aspartate and alanine transaminases, acid and alkaline phosphatases and aldolase. It was observed that the activities of aspartate aminotransferase and alkaline phosphatase reached their maxima in July and alanine transaminase in May. The activities of acid phosphatase and aldolase showed their minima in July. Comparing these data with the literature it was noted that t...
Natural protease inhibitors: qualitative and quantitative assay by fibrinogen-agarose electrophoresis.
Analytical biochemistry    May 1, 1984   Volume 138, Issue 2 335-339 doi: 10.1016/0003-2697(84)90818-2
Pellegrini A, Hägeli G, Fretz D, von Fellenberg R.An electrophoretic procedure for the qualitative and quantitative assay of protein protease inhibitors is reported. This assay is particularly suited for investigations of crude biological materials when specific antisera are not available. The supporting medium consists of agarose into which denatured fibrinogen is incorporated as the substrate for proteases. The processing then is divided into two steps: (1) electrophoretic resolution of the inhibitor containing material and (2) detection of the inhibitor bands through their protease inhibiting activity. The inhibitor position is thus made v...
Sequence of the high-activity equine erythrocyte carbonic anhydrase: N-terminal polymorphism (acetyl-Ser/acetyl-Thr) and homologies to similar mammalian isozymes.
Biochemical genetics    April 1, 1984   Volume 22, Issue 3-4 357-367 doi: 10.1007/BF00484234
Jabusch JR, Deutsch HF.The amino acid sequence of the high-activity equine erythrocyte carbonic anhydrase (CA-II) has been determined. Two different N-termini are noted, the C1 form having an N-acetyl-serine and the C2 form an N-acetyl-threonine. The sequence of the equine enzyme is most homologous to the human CA-II isozyme, with 224 of the 259 residues being identical.
Alpha 2-macroglobulin from horse plasma. Purification, properties and interaction with certain serine proteinases.
Biochemistry international    April 1, 1984   Volume 8, Issue 4 589-596 
Dubin A, Potempa J, Silberring J.alpha 2-macroglobulin was isolated by polyethylene glycol precipitation, gel filtration on Sephacryl S-300 and DE-52 cellulose chromatography, with 20% yield. The preparation obtained was homogenous as tested by biochemical and immunological criteria. Its molecular mass was estimated at 800,000, comprising of four identical subunits. The isoelectric point of our preparation was 4.8 and two molecules of serine proteinases per 1 molecule of inhibitor were bound.
[An analysis of reproducibility in the determination of the activity of selected enzymes in the blood serum of horses].
Veterinarni medicina    March 1, 1984   Volume 29, Issue 3 163-170 
Kovár J.Single biochemical analyses can be used for the diagnosis of animal diseases only with the knowledge of the effects that may distort the single result. The study of the repeatability of analyses is described in the four basic enzymes (AST, ALP, GMT, LD), which are most frequently used for diagnosis. The experiment was conducted in a group of ten Kladrub mares. Six blood samples were taken from each of the mares within ten days. The measured values were subjected to statistical processing and repeatability coefficients (r op) were calculated. All the r op values were high (ALP--0.96, LD--0.93, ...
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