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.
The elimination of injected superoxide dismutase from synovial fluid of the horse.
Australian veterinary journal    April 1, 1989   Volume 66, Issue 4 117-119 doi: 10.1111/j.1751-0813.1989.tb09763.x
Auer DE, Ng JC, Hrdlicka J, Seawright AA.No abstract available
Synthesis and aromatization of 19-norandrogens in the stallion testis.
Journal of steroid biochemistry    April 1, 1989   Volume 32, Issue 4 537-544 doi: 10.1016/0022-4731(89)90387-7
Dintinger T, Gaillard JL, Zwain I, Bouhamidi R, Silberzahn P.The results of the measurement of 19-nortestosterone in the testiscular artery and vein of the stallion, the very low levels of this steroid in the peripheral blood of geldings and the similar patterns of increase in the peripheral levels of 19-nortestosterone and testosterone after hCG stimulation, show that 19-nortestosterone, like testosterone, is essentially synthesized in the testis. This testicular origin was confirmed by the ability of testicular tissue to synthesize 19-norandrogens from [4-14C]androgens in vitro. 19-Nortestosterone was 50% conjugated in the peripheral blood and almost ...
Induction of equine postanesthetic myositis after halothane-induced hypotension.
American journal of veterinary research    March 1, 1989   Volume 50, Issue 3 404-410 
Lindsay WA, Robinson GM, Brunson DB, Majors LJ.Wick catheters were used to measure intracompartmental pressures of the extensor carpi radialis muscles and long heads of the triceps brachii muscles of 7 horses maintained under halothane anesthesia during controlled ventilation. Horses were positioned in left lateral recumbency on a water bed for 4 hours. Using a crossover design, 6 of the 7 horses were subjected to normotensive and hypotensive anesthesia on separate occasions. Hypotension was achieved by increasing the inspired halothane concentration. Hematologic and biochemical measurements were determined at designated intervals before, ...
Analysis of N-acetyl-4-O-acetylneuraminic-acid-containing N-linked carbohydrate chains released by peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase F. Application to the structure determination of the carbohydrate chains of equine fibrinogen.
European journal of biochemistry    March 1, 1989   Volume 180, Issue 1 101-110 doi: 10.1111/j.1432-1033.1989.tb14620.x
Damm JB, Voshol H, Hård K, Kamerling JP, Vliegenthart JF.The carbohydrate chains of equine fibrinogen were enzymatically released by peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase F. The oligosaccharides obtained were fractionated by a combination of FPLC and HPLC and analyzed by 500-MHz 1H-NMR spectroscopy. Four monosialo and four disialo diantennary N-acetyllactosamine type of carbohydrate chains occur: (formula; see text)
A monoclonal antibody against horse kidney (Na+ + K+)-ATPase inhibits sodium pump and E2K to E1 conversion of (Na+ + K+)-ATPase from outside of the cell membrane.
Biochimica et biophysica acta    February 2, 1989   Volume 994, Issue 2 104-113 doi: 10.1016/0167-4838(89)90149-0
Satoh K, Nakao T, Nagai F, Kano I, Nakagawa A, Ushiyama K, Urayama O, Hara Y, Nakao M.Monoclonal antibodies against horse kidney outer medulla (Na+ + K+)-ATPase were prepared. One of these antibodies (M45-80), was identified as an IgM, recognized the alpha subunit of the enzyme. M45-80 had the following effects on horse kidney (Na+ + K+)-ATPase: (1) it inhibited the enzyme activity by 50% in 140 mM Na+ and by 80% in 8.3 mM Na+; (2) it increased the Na+ concentration necessary for half-maximal activation (K0.5 for Na+) from 12.0 to 57.6 mM, but did not affect K0.5 for K+; (3) it slightly increased the K+-dependent p-nitrophenylphosphatase (K-pNPPase) activity; (4) it inhibited p...
Studies on serum selenium and tocopherol in white muscle disease of foal.
Nihon juigaku zasshi. The Japanese journal of veterinary science    February 1, 1989   Volume 51, Issue 1 52-59 doi: 10.1292/jvms1939.51.52
Higuchi T, Ichijo S, Osame S, Ohishi H.In order to clarify the cause of white muscle disease (W.M.D.) in foals, tocopherol and selenium concentrations in serum and glutathione peroxidase activities in blood were measured. Examination was made on the samples from horses affected with W.M.D., the foal kept with them in the same stable, the foals kept in the stables without affected foals, and respective mares. The heavy-breed horses in Fukuoka prefecture and Tokachi district were also examined for comparison. Serum tocopherol levels of these foals were normal because after intake of colostrum. Mares of affected foals showed lower toc...
Steroids in equine testes: the identification of endogenous 19-hydroxy and 19-nor neutral steroids by gas chromatography–mass spectrometry.
The Journal of endocrinology    February 1, 1989   Volume 120, Issue 2 223-229 doi: 10.1677/joe.0.1200223
Dumasia MC, Houghton E, Jackiw M.After homogenization of testicular tissue from stallions aged 1, 2 and 5 years, the unconjugated and conjugated steroids were isolated by a combined solvent-solid extraction procedure. The conjugates were further separated into glucuronides and sulphates by chromatography using Sephadex LH-20. After enzyme hydrolysis and solvolysis of the respective conjugate classes, the three extracts, unconjugated steroids, aglycones and solvolysed sulphates, were purified by chromatography using Kieselgel 60H columns. Five fractions were resolved from each extract; an aliquot of each fraction was derivatiz...
Crystallization and preliminary X-ray study of horse pancreatic lipase.
Journal of molecular biology    January 5, 1989   Volume 205, Issue 1 259-261 doi: 10.1016/0022-2836(89)90380-x
Lombardo D, Chapus C, Bourne Y, Cambillau C.Horse (Equus caballus) pancreatic lipase (EC 3.1.1.3) has been crystallized using the hanging drop method of vapour diffusion at 20 degrees C. The best crystals were grown from an 8 mg/ml solution in 10 to 20% (w/v) polyethylene glycol 8000, 10 mM-MgCl2, 0.1 M-NaCl, 0.1 M-Mes buffer (pH 5.6). They reach dimensions of 0.8 mm x 0.4 mm x 0.6 mm. X-ray examination of the lipase crystals shows that they are orthorombic with a space group P2(1)2(1)2(1). Their cell dimensions are a = 79.8 A, b = 97.2 A c = 145.3 A. Two molecules per asymmetric unit give a Vm value of 2.82 A3/dalton (56% water content...
The structure and properties of horse muscle acylphosphatase in solution. Mobility of antigenic and active site regions.
FEBS letters    January 2, 1989   Volume 242, Issue 2 225-232 doi: 10.1016/0014-5793(89)80474-0
Saudek V, Williams RJ, Ramponi G.The solution structure of acylphosphatase determined by proton nuclear magnetic resonance spectroscopy is described. The results allow us to discuss the fold of the protein (101 amino acids), to correlate the exposure and the mobility of the backbone with the antigenicity, and to locate the active site.
Immunocytochemical localization of carbonic anhydrase isozyme III in equine thymus.
Histochemistry    January 1, 1989   Volume 91, Issue 1 39-42 doi: 10.1007/BF00501908
Nishita T, Matsushita H.Sections of equine thymus were examined for the presence of carbonic anhydrase (CA) isozymes by an immunohistochemical method. Carbonic anhydrase III, a major enzyme of skeletal muscle, was localized in some of the epithelial-reticular cells of the equine thymus. This finding suggests the presence of a new type of cell in the thymic cortex. The concentration of CA-III in the thymus was 17 micrograms/g wet tissue. CA-I and CA-II were not found in equine thymus.
[Histochemical changes in skeletal muscles of racehorses susceptible to rhabdomyolysis after exertion. I. Early myopathological changes].
Acta histochemica    January 1, 1989   Volume 87, Issue 1 1-11 
Meijer AE, van den Hoven R, Wensing T, Breukink HJ.In this communication, the results of an enzyme histochemical study on m. gluteus medius of horses, sensitive to exertional myopathy, during attacks of rhabdomyolysis are presented. The activity and location of about 25 enzymes were examined. In the present report, the early metabolic changes are discussed. Within 6 min after an attack, some large rounded fibres (approximately 2%) were seen, which showed an intense red staining in the haematoxylin and eosin sections. These hypercontracted fibres showed an increase in activity of mitochondrial adenosine triphosphatase, indicating the presence o...
Methylation at the CpG doublet in equine adenovirus genome.
Research in veterinary science    January 1, 1989   Volume 46, Issue 1 129-130 
Harasawa R, Higashi T.Viral DNA obtained from the equine adenovirus propagated in equine transitional cell carcinoma (ETCC) cells and in equine fetal dermis cells were compared by cleaving with isoschizomeric restriction enzymes, HpaII and MspI, and then electrophoresed in 1.4 per cent agarose gels. Differences between the HpaII and MspI cleavage patterns were evident in viral DNA obtained only from the equine adenovirus propagated in ETCC cells, suggesting site specific methylation at CpG sequences.
Comparative microsomal oxidation of febantel and its metabolite fenbendazole in various animal species.
Xenobiotica; the fate of foreign compounds in biological systems    January 1, 1989   Volume 19, Issue 1 97-100 doi: 10.3109/00498258909034681
Montesissa C, Stracciari JM, Fadini L, Beretta C.A comparison has been made of the in vitro metabolism of febantel (FBT) with that of one of its pharmacologically active metabolites fenbendazole (FBZ) using microsomal preparations from liver of sheep, calf, horse, pig, rat, chicken and trout. The oxidation of FBT to the corresponding sulphoxide appeared to be far more rapid with the exception of the trout, than a similar reaction with FBZ. Indeed FBT was further metabolized in several species by cyclization and further oxidation. This observation could have toxicological significance in view of the greater tetratogenic effects of the metabol...
Muscular adaptation of horses during intensive training and detraining.
Equine veterinary journal    January 1, 1989   Volume 21, Issue 1 27-33 doi: 10.1111/j.2042-3306.1989.tb02085.x
Essén-Gustavsson B, McMiken D, Karlström K, Lindholm A, Persson S, Thornton J.Five horses were studied during a five-week regime of controlled intensive daily training on a high-speed treadmill followed by five weeks of detraining. Muscle biopsies were taken weekly from both the right and left gluteus muscle and from the sternocephalicus muscle before, and at the end of, the training and detraining periods. Histochemical and biochemical analyses of the sternocephalicus muscle showed no metabolic adaptation with either training or detraining. No significant differences were observed in any of the analysed parameters in the gluteus muscle between contralateral sites. Glyc...
Application of an affinity electrophoretic and in situ oxidation method to the study of the equine protease inhibitory proteins.
Electrophoresis    January 1, 1989   Volume 10, Issue 1 40-45 doi: 10.1002/elps.1150100110
Patterson SD, Bell K.An affinity method was developed to investigate the interaction between protease and protease inhibitor by incorporating a protease incubation step into a two-dimensional electrophoretic separation of the plasma protease inhibitory proteins. This involved the application of the isoelectric focusing gel to filter paper saturated in the protease of choice before being placed on the second-dimensional polyacrylamide electrophoresis gel. General protein staining or immunoblotting was used to detect the protein or ligand in the complex. An in situ oxidation method was developed using the reagent ch...
Purification of F(ab’)2 anti-snake venom by caprylic acid: a fast method for obtaining IgG fragments with high neutralization activity, purity and yield.
Toxicon : official journal of the International Society on Toxinology    January 1, 1989   Volume 27, Issue 3 297-303 doi: 10.1016/0041-0101(89)90177-3
dos Santos MC, D'Império Lima MR, Furtado GC, Colletto GM, Kipnis TL, Dias da Silva W.Pooled horse plasma containing antibodies against Crotalus durissus terrificus whole venom were digested with pepsin at an enzyme-substrate ratio of 8:1, pH 3.1, for 40 min and the F(ab')2M fragments purified by adding 8.7% caprylic acid (pH 5.0). For comparison, F(ab')2B purified by precipitation with ammonium sulphate and uncleaved IgG purified with caprylic acid were also prepared. Fab' fragments were obtained by reduction and alkylation of F(ab')2B. The anti-whole C.d. terrificus venom titers, determined by Dot-Blot were 12,800 (IgG), 6400 [F(ab')2B], 4800 [F(ab')2M] and 3200 (Fab'B). Immu...
[Performance testing of mules and Haflinger horses used as pack animals].
DTW. Deutsche tierarztliche Wochenschrift    January 1, 1989   Volume 96, Issue 1 17-20 
von Rennenkampff F, Kraft H.During 20 weeks blood constituents in peripheral blood (Erythrocyte count, Packed cell volume, Hemoglobin, Sedimentation rate, activities of Aspartate aminotransferase, Alanine aminotransferase, Creatine phosphokinase, Lactate dehydrogenase, Lactate dehydrogenase-1-isoenzyme, Glucose, Lactate, Total bilirubin), pulse and respiration rate were determined at rest and after exercise. Significant increase of blood values after exercise could be noted in relation to the intensity of exercise and the performance of the animals. The well trained horses had an increase of their performance according t...
Kinetic and inhibitory characteristics of serum angiotensin-converting enzyme from nine mammalian species.
Comparative biochemistry and physiology. B, Comparative biochemistry    January 1, 1989   Volume 92, Issue 2 399-403 doi: 10.1016/0305-0491(89)90300-3
Ibarra-Rubio ME, Pena JC, Pedraza-Chaverri J.1. Serum angiotensin-converting enzyme activities were obtained from nine mammalian species: rat, mouse, horse, sheep, guinea pig, hamster, rabbit, dog and man. 2. Kinetic constants (Km and Vmax) using hippuryl-L-histidyl-L-leucine as substrate and inhibitory constants (I50 and Ki) for captopril were determined for the serum ACE of each species. 3. There were important differences in the kinetic and inhibitory constants (Kms went from 6.6 mM to 1.21 mM for hamster and guinea pig; I50 ranged from 2100 nM to 3 nM for mouse and sheep) as well as differences in enzyme activity of the different spe...
[Experimental equine fascioliasis: evolution of serologic, enzymatic and parasitic parameters].
Annales de recherches veterinaires. Annals of veterinary research    January 1, 1989   Volume 20, Issue 3 295-307 
Soulé C, Boulard C, Levieux D, Barnouin J, Plateau E.Three, four, and one horses were respectively infected with 100, 1,000, and 5,000 metacercariae of Fasciola hepatica. Six of them were reinfected 38 weeks later with 1,000 metacercariae each. Specific antibodies assayed by counter-electrophoresis, passive hemagglutination and ELISA tests appeared three to six weeks post-infection and peaked 10 to 17 weeks post-infection. Horses infected by 1,000 metacercariae and more showed 17.6% of positive samples by counter-electrophoresis, 49.2% by ELISA, and 75.6% by passive hemagglutination. Plasma glutamate dehydrogenase and gamma-glutamyltransferase l...
Enzymatic deacylations of esterified saccharides–III. Comparison of de-esterifications by serum esterases from different sources.
Comparative biochemistry and physiology. B, Comparative biochemistry    January 1, 1989   Volume 92, Issue 4 681-684 doi: 10.1016/0305-0491(89)90249-6
Tomić S, Sesartić L, Tomasić J.1. 14C-labelled methyl 2,6-di-O-pivaloyl-alpha-D-glucopyranoside (1) was used as a substrate for esterases from rabbit, guinea pig, mouse, donkey, pig, horse, sheep and human sera. 2. Stepwise de-esterification of the diester substrate 1 occurred with rabbit, guinea pig and mouse serum. Data on time-course experiments and kinetic data are reported. 3. The use of donkey, pig, horse, sheep and human serum led to the migration of the 2-O-pivaloyl group in substrate 1 to the position 4- in the sugar molecule, followed by stepwise de-esterifications of both 1 and the newly formed methyl 4,6-di-O-pi...
[Histochemical changes in skeletal muscles of racehorses susceptible to rhabdomyolysis after exertion. II. Later myopathological and regeneration phenomena].
Acta histochemica    January 1, 1989   Volume 87, Issue 1 13-21 
Meijer AE, van den Hoven R, Wensing T, Breukink HJ.Needle biopsies from m. gluteus medius of 22 horses which had suffered from repeated attacks of exertional myopathy were studied at various times after an attack, to determine if metabolic alterations can be demonstrated by enzyme histochemistry. Morphological changes and activity of 25 enzymes were studied. Immediately after onset of an attack, some large rounded fibres with a defect of the oxidative phosphorylation were seen. After some hours these fibres lost their glycolytic enzyme activity, followed by disappearance of mitochondrial enzyme activity with accumulation of Ca2+-containing sub...
A comparative study on acetyl-CoA synthesising enzymes in spinal cord from cows, horses and pigs.
Comparative biochemistry and physiology. C, Comparative pharmacology and toxicology    January 1, 1989   Volume 93, Issue 2 201-206 doi: 10.1016/0742-8413(89)90221-1
Björkman C.1. Comparative data are presented of the activities of pyruvate dehydrogenase complex and acetyl-CoA synthetase and of the acetate content in homogenates from ventral grey matter in spinal cord from cows and two non-ruminant species, pigs and horses. The methods used in the study are evaluated and discussed. 2. The total pyruvate dehydrogenase complex activity was 24.9-29.9 mU/mg protein and did not differ between the species. The part of the complex that was in active form at the sampling occasion was 60, 85 and 95% in cows, pigs and horses, respectively. 3. Acetyl-CoA synthetase activity dif...
Evolution of the herpes thymidine kinase: identification and comparison of the equine herpesvirus 1 thymidine kinase gene reveals similarity to a cell-encoded thymidylate kinase.
Nucleic acids research    December 9, 1988   Volume 16, Issue 23 11303-11317 doi: 10.1093/nar/16.23.11303
Robertson GR, Whalley JM.We have identified the equine herpesvirus 1 (EHV-1) thymidine kinase gene (TK) by DNA-mediated transformation and by DNA sequencing. Alignment of the amino acid sequence of the EHV-1 TK with the TKs from 3 other herpesviruses revealed regions of homology, some of which correspond to the previously identified substrate binding sites, while others have as yet, no assigned function. In particular, the strict conservation of an aspartate within the proposed nucleoside binding site suggests a role in ATP binding for this residue. Comparison of 5 herpes TKs with the thymidylate kinase of yeast revea...
The use of enzyme profiles in the training and racing of horses: a review.
Journal of the South African Veterinary Association    December 1, 1988   Volume 59, Issue 4 213-214 
Gummow B, Reyers F.The effects of age, training, racing and endurance riding on serum enzyme profiles in the horse are reviewed and discussed.
Physical and chemical characterization of a horse serum carboxylesterase.
Archives of biochemistry and biophysics    November 15, 1988   Volume 267, Issue 1 271-279 doi: 10.1016/0003-9861(88)90032-x
Torres JL, Rush RS, Main AR.The serine carboxylesterase from horse serum was characterized by amino acid composition, peptide mapping, molecular and subunit weights, and sequencing of the amino acids around the essential serine residue at the active site. A protocol was developed for using reversed-phase high-performance liquid chromatography as the final step to obtain homogeneous preparations of horse serum carboxylesterase. Amounts sufficient for determining the amino acid composition and for peptide maps were obtained from a partially purified starting material which contained approximately 55% carboxylesterase. The ...
The primary structure of donkey (Equus asinus) lysozyme contains the Ca(II) binding site of alpha-lactalbumin.
Biological chemistry Hoppe-Seyler    October 1, 1988   Volume 369, Issue 10 1109-1115 doi: 10.1515/bchm3.1988.369.2.1109
Godovac-Zimmermann J, Conti A, Napolitano L.The complete primary structure of donkey lysozyme has been established by pulsed liquid-phase sequencing of tryptic and chymotryptic peptides isolated by RP-HPLC. The positions of the Cys residues were identified by labeling the Cys residues with DABIA-reagent. Donkey lysozyme is a c-type lysozyme which is 129 amino acids long. It exhibits 50% homology to the human protein. We observe the full Ca(II) binding site suggested for the homologous alpha-lactalbumines. Although horse lysozyme has been reported to contain asparagine in position 61, which was in conflict with the three-dimensional stru...
The effect of drugs used in the treatment of osteoarthrosis on stromelysin (proteoglycanase) of equine synovial cell origin.
Equine veterinary journal. Supplement    September 1, 1988   Issue 6 28-32 doi: 10.1111/j.2042-3306.1988.tb04645.x
May SA, Hooke RE, Lees P.There is increasing evidence that the proteoglycan-degrading neutral metalloproteinase, stromelysin, is a key enzyme in the pathogenesis of osteoarthrosis. Equine synovial lining cells were stimulated in vitro to produce stromelysin, and phenylbutazone, flunixin, betamethasone, sodium hyaluronate and polysulphated glycosaminoglycan (PSGAG) were tested for their ability to inhibit the action of this enzyme on 14C-labelled casein substrate. Only PSGAG possessed inhibitory activity at concentrations likely to be achieved therapeutically in the equine fetlock joint.
In vitro evaluation of a sustained-release veterinary peroral pellet preparation.
Journal of pharmaceutical sciences    September 1, 1988   Volume 77, Issue 9 757-759 doi: 10.1002/jps.2600770907
Ritschel WA, Agrawala P, Kraeling M, Sathyan G, Berger K.In a preceding in vivo study in horses, wide interindividual variation was found in the extent of bioavailability and time to reach peak concentration after peroral administration of one specific theophylline sustained-release dosage form. The purpose of the present study was to investigate the factors of potency, the pH of dissolution medium, the enzymes in the dissolution medium, and the crushing of the pellets on in vitro performance. The results show a wide variation in potency for the individual units, an increase in release rate with increasing pH, and an increase in release rate if the ...
Cytochrome c: ion binding and redox properties. Studies on ferri and ferro forms of horse, bovine, and tuna cytochrome c.
The Journal of biological chemistry    August 25, 1988   Volume 263, Issue 24 11652-11656 
Gopal D, Wilson GS, Earl RA, Cusanovich MA.The ion binding properties of horse, bovine, and tuna cytochrome c (both oxidized and reduced) have been measured using a combination of ultrafiltration, neutron activation, and ion chromatography. The ions investigated were chloride, phosphate, and Tris-cacodylate. Ion chromatography and neutron activation analysis techniques were employed to determine the concentration of free anions. Binding constants are obtained from modified Scatchard plots (in the range of 10-2000 M-1). The redox potentials for cytochrome c at different ionic strengths, pH 7.0, have been determined. In this paper we rep...
Horse brain acylphosphatase: purification and characterization.
FEBS letters    August 15, 1988   Volume 236, Issue 1 209-216 doi: 10.1016/0014-5793(88)80316-8
Stefani M, Berti A, Camici G, Manao G, Degl'Innocenti D, Prakash G, Marzocchini R, Ramponi G.Two structurally different acylphosphatases found in horse brain were purified; they were not immunologically related. The molecular masses were almost identical and the kinetic parameters were rather similar. The data reported indicate that one of the purified brain acylphosphatases and an enzyme, previously isolated from horse muscle, are the same protein. The presence of this acylphosphatase form in the brain has not been reported before. The other acylphosphatase seemed to be the same as the enzyme which had been purified from calf brain and partially characterized by Diederich and Grisoli...
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