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.
Mammalian ribonucleases. The absence of a glycosylated Asn-Pro-Thr sequence in horse ribonuclease and the presence of tryptophan at position 39 in horse and dromedary ribonuclease.
FEBS letters    June 3, 1985   Volume 185, Issue 1 115-120 doi: 10.1016/0014-5793(85)80752-3
Beintema JJ.Parts of the amino acid sequences of horse and dromedary pancreatic ribonuclease were reinvestigated. The sequence of residues 21-25 in horse ribonuclease is Ser-Asn-Pro-Thr-Tyr or Ser-Asn-Ser-Thr-Tyr. The asparagine in the latter sequence is glycosylated. Horse ribonuclease possesses four additional amino acid residues at the C-terminus, like a number of other ribonucleases. Position 39 in horse and dromedary ribonuclease is not deleted but is occupied by tryptophan.
The amino-acid sequence of beta-lactoglobulin II from horse colostrum (Equus caballus, Perissodactyla): beta-lactoglobulins are retinol-binding proteins.
Biological chemistry Hoppe-Seyler    June 1, 1985   Volume 366, Issue 6 601-608 doi: 10.1515/bchm3.1985.366.1.601
Godovac-Zimmermann J, Conti A, Liberatori J, Braunitzer G.beta-Lactoglobulin isolated from horse colostrum is heterogeneous and contains two components: beta-lactoglobulin I and beta-lactoglobulin II. These two proteins are monomeric and show differences in their electrophoretic mobilities, chain lengths and primary structures. The complete amino-acid sequence of beta-lactoglobulin II was determined by automated Edman degradation of the intact protein and of the peptides derived from these by digestion with trypsin or chymotrypsin and by chemical cleavage with cyanogen bromide. Unlike other beta-lactoglobulins which contain 162 amino acids, horse bet...
Failure of superoxide dismutase to alter equine arachidonic acid-induced platelet aggregation, in vitro or ex vivo.
American journal of veterinary research    May 1, 1985   Volume 46, Issue 5 1104-1106 
Clemmons RM, Lee MR, Bliss EL, Asbury AC, Cook D, Brown V.Superoxide dismutase (SOD), a free radical scavenger with anti-inflammatory activity, was administered IM to horses. Ex vivo platelet aggregation in response to arachidonic acid was monitored to determine whether exogenous SOD altered equine platelet prostaglandin metabolism. Preparations of platelet-rich plasma obtained before SOD administration were incubated with different concentrations of SOD and were aggregated with arachidonic acid. Superoxide dismutase did not exert a demonstrable effect, either ex vivo or in vitro. Aspirin abolished arachidonic acid-induced platelet aggregation in vit...
Antigenic determinants of acylphosphatase from porcine skeletal muscle.
Journal of biochemistry    April 1, 1985   Volume 97, Issue 4 1143-1154 doi: 10.1093/oxfordjournals.jbchem.a135159
Kizaki T, Mizuno Y, Takasawa T, Shiokawa H.Analysis of the quantitative precipitin reaction of acylphosphatase from porcine skeletal muscle with rabbit antiserum indicated the presence of at least two antigenic determinants on the porcine enzyme molecule. Immunological cross-reactivities of acylphosphatases from equine and rabbit skeletal muscles were examined. In double immunodiffusion with the antiserum, the precipitin lines of the porcine and equine enzymes completely fused, while the rabbit enzyme gave no precipitin line. The reaction between the 125I-labeled porcine enzyme and its antibody was inhibited to the same extent by the p...
[Hyalurodinase activity of beta-hemolytic streptococci of the Lancefield group C]. Balke E, Weiss R, Seipp A.A total of 110 strains of beta-hemolytic streptococci, belonging to serogroup C (Lancefield), isolated from horses (71 S. zooepidemicus, 27 S. equisimilis and 12 S. equi) as well as 5 reference strains were tested for their ability to produce hyaluronidase. The determinations were carried out in a culture test on agarose gel and in a liquid test system (turbidity test according to DiFerrante). The results of both methods used showed that the three Streptococcus species could be differentiated by the relative quantitative determination of hyaluronidase activity. S. equisimilis strains produce 5...
Inhibition of lipases by proteins. A kinetic study with dicaprin monolayers.
The Journal of biological chemistry    February 25, 1985   Volume 260, Issue 4 2268-2273 
Gargouri Y, Pieroni G, Rivière C, Sugihara A, Sarda L, Verger R.We report further investigations on protein inhibition of pancreatic and microbial lipases carried out with the monolayer technique. When beta-lactoglobulin A, melittin, serum albumin, myoglobin, and a protein inhibiting lipase from soybean were preincubated with a dicaprin film at a surface pressure of 35 dynes/cm, no activity was detected with horse pancreatic or Rhizopus delemar lipases. By contrast, Rhizopus arrhizus and Geotrichum candidum lipase activities were not impaired under the same conditions. Experiments using mixed lipid-protein film transfer clearly show that the inhibition of ...
Native and carboxymethylated horse liver alcohol dehydrogenase: electrostatic fields and the Pauling strain-distortion hypothesis.
Progress in clinical and biological research    January 1, 1985   Volume 174 169-179 
Dunn MF, Dahl KH.No abstract available
Activity of delta(5)3beta-hydroxysteroid dehydrogenase and steroid hormones content in early preimplantation horse embryos.
Folia histochemica et cytobiologica    January 1, 1985   Volume 23, Issue 1-2 81-84 
Paulo E, Tischner M.The activity of delta (5)3 beta-hydroxysteroid dehydrogenase was examined histochemically in 6 to 10 days aged horse blastocysts. A positive reaction was noted in the blastomeres of all embryos incubated in medium with substrate. Measurable amounts of progesterone, androgens and estrogens were found in blastocysts on day 8th. The presence of enzyme and hormones suggests that steroid hormone production takes place in very early preimplantation horse embryos.
[Clinical signs, enzyme activity and antibody formation in experimental sarcosporidia infections of horses]. Schnieder T, Zimmermann U, Matuschka FR, Bürger HJ, Rommel M.No abstract available
Influence of several perturbants on the rate of autoxidation of horse heart ferrocytochrome c.
The International journal of biochemistry    January 1, 1985   Volume 17, Issue 1 119-122 doi: 10.1016/0020-711x(85)90095-3
Harrington JP, Carrier TL.The effect of several different types of perturbants and pH on the rate of autoxidation of horse heart ferrocytochrome c was investigated. The kinetic behavior is unique to each perturbant used. Rates of autoxidation followed first-order kinetics over the time span (0-180 min) studied. The Cl- and Br- anions exhibit an initial increase in the rate of autoxidation up to 100 mM, followed by a decrease in kinetics at 500 mM anion concentration. The ClO4- anion exhibits only an increase in the rate of autoxidation with increasing ionic strength, where as, propylurea, a hydrophobic perturbant, is n...
Distribution of enzymes of purine metabolism in lymphocytes of horse, Equus caballus.
Comparative biochemistry and physiology. B, Comparative biochemistry    January 1, 1985   Volume 81, Issue 2 459-465 doi: 10.1016/0305-0491(85)90342-6
Magnuson NS, Perryman LE, Mason PH, Marta KM.A microassay requiring as few as 2 X 10(5) cells per assay was developed for systematic analysis of 9 purine enzymes in lymphocytes from equine peripheral blood, spleen, lymph node, thymus and bone marrow. The activities of adenosine deaminase (ADA), purine nucleoside phosphorylase (PNP), adenosine kinase (AK), deoxyadenosine kinase (dAK), deoxycytidine kinase (dCK), 5'-nucleotidase (5'-N), AMP deaminase, hypoxanthine-guanine phosphoribosyl transferase (HGPRT or HPRT), and adenine phosphoribosyl transferase (APRT) were measured by this microassay in lymphocytes from peripheral blood from four ...
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...
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