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.
Alkaline isomerization of ferricytochrome c: identification of the lysine ligand.
Proceedings of the National Academy of Sciences of the United States of America    July 1, 1974   Volume 71, Issue 7 2892-2894 doi: 10.1073/pnas.71.7.2892
Wilgus H, Stellwagen E.Changes in the visible absorbance spectra of complexes of horse heart cytochrome c hemopeptide 1-65, peptide 66-104, and their guanidinated counterparts are compared with those characteristic of native and fully guanidinated ferricytochrome c over the pH range 7 to 11. Upon raising the pH, the methionine ligand in the guanidinated hemopeptide 1-65.peptide 66-104 complex is replaced by a strong field ligand. By contrast, the methionine ligand in the hemopeptide 1-65.guanidinated peptide 66-104 is replaced by a weak field ligand. These results demonstrate that lysine 13 does not ligate with the ...
Stimulation by thyrotropin of horse thyroid plasma membranes adenylate cyclase: evidence of cooperativity.
Biochemical and biophysical research communications    May 20, 1974   Volume 58, Issue 2 446-453 doi: 10.1016/0006-291x(74)90385-4
Boeynaems JM, Pochet R, Dumont JE.No abstract available
A cupro-zinc protein with superoxide dismutase activity from horse liver. Isolation and properties.
Comparative biochemistry and physiology. B, Comparative biochemistry    April 15, 1974   Volume 47, Issue 4 767-777 doi: 10.1016/0305-0491(74)90022-4
Albergoni V, Cassini A.No abstract available
The relation between adenylate cyclase activation and cAMP acculumation in the horse thyroid gland stimulated by thyrotropin.
Molecular and cellular endocrinology    April 1, 1974   Volume 1, Issue 2 139-155 doi: 10.1016/0303-7207(74)90006-9
Boeynaems JM, Van Sande J, Pochet R, Dumont JE.No abstract available
Proceedings: Inhibition of acetylcholine deactivating enzymes of the horse plasma by heavy metals and arsenic.
Naunyn-Schmiedeberg's archives of pharmacology    March 22, 1974   Volume 282, Issue Suppl R84 
Schmid A, Mayer D, Raake W.No abstract available
Multiple components of beta-N-acetylhexosaminidase from equine kidney. Their action on glycolipids and allied oligosaccharides.
Journal of biochemistry    March 1, 1974   Volume 75, Issue 3 495-507 doi: 10.1093/oxfordjournals.jbchem.a130418
Seyama Y, Yamakawa T.No abstract available
Erythrocytic ouabain-sensitive and ouabain-insensitive adenosine triphosphatase in various mammalian species;
Comparative biochemistry and physiology. A, Comparative physiology    March 1, 1974   Volume 47, Issue 3 1123-1126 doi: 10.1016/0300-9629(74)90485-x
Gupta JD, Peterson VJ, Harley JD.No abstract available
Protein phosphokinase activity in horse thyroid nuclei.
Archives internationales de physiologie et de biochimie    February 1, 1974   Volume 82, Issue 1 207 
Verhaegen M, Sand G.No abstract available
Proceedings: The effects of exogenous gonadotrophins on ovarian adenyl cyclase activity.
Journal of reproduction and fertility    February 1, 1974   Volume 36, Issue 2 445-446 doi: 10.1530/jrf.0.0360445
Nugent CL, Lopata A, Gould MK.No abstract available
Fractionation of iodinated particles and mitochondria from thyroid by zonal centrifugation and a study of their heterogeneity.
The Biochemical journal    February 1, 1974   Volume 138, Issue 2 299-304 doi: 10.1042/bj1380299
Miquelis R, Simon C.1. The subcellular particles of horse and rat thyroids were fractionated in a B XIV zonal rotor on a non-linear gradient of Ficoll after labelling with radioactive iodine in vitro (horse) or in vivo (rat). In the horse, the resulting fractions were analysed for radioactive iodine, protein and enzymes representative of certain subcellular particles. In the rat, iodine turnover and thyrotrophin stimulation were studied. 2. The population of iodinated particles could be subdivided into three main classes, characterized by differences in beta-galactosidase and acid phosphatase content and position...
On the limited peptic digestion of horse heart cytochrome C. isolation of C-terminal peptide sequences.
International journal of peptide and protein research    January 1, 1974   Volume 6, Issue 3 145-148 doi: 10.1111/j.1399-3011.1974.tb02371.x
Fontana A, Vita C, Toniolo C.No abstract available
Acute rhabdomyolysis (“tying-up”) in standardbred horses. A morphological and biochemical study.
Acta veterinaria Scandinavica    January 1, 1974   Volume 15, Issue 3 325-339 doi: 10.1186/BF03547462
Lindholm A, Johansson HE, Kjaersgaard P.LINDHOLM, A., H.-E. JOHANSSON & P. KJÆRSGAARD: Acute rhabdomyolysis (“tying-up”) in standardbred horses. A morphological and biochemical study. Acta vet. scand. 1974, 15, 325–339. — Morphological, biochemical and histochemical changes were studied in muscle needle biopsy specimens (gluteus medius) from 59 standardbred trotters with acute clinical symptoms of the “tying-up” disease. All horses had increased levels of serum enzymes SGOT and SCPK. The biopsy specimens were taken at various intervals after onset of clinical symptoms (1–4 hrs., 18–24 hrs. and 2–20 days). Ry light...
The development and distribution of alkaline phosphatase activity in the small intestine of the horse.
Research in veterinary science    January 1, 1974   Volume 16, Issue 1 110-111 
Roberts MC.No abstract available
Proceedings: Inhibitory effect of calcium on adenyl cyclase from horse parathyroid.
Calcified tissue research    January 1, 1974   Volume 15, Issue 2 167-168 
Matsuzaki S, Dumont JE.No abstract available
Fibre composition, enzyme activity and concentrations of metabolites and electrolytes in muscles of standardbred horses.
Acta veterinaria Scandinavica    January 1, 1974   Volume 15, Issue 3 287-309 doi: 10.1186/BF03547460
Lindholm A, Piehl K.LINDHOLM, ARNE and KARIN PIEHL: Acta vet. scand. 1974, , 287–309. — Measurements of metabolites, electrolytes, water, RNA and protein concentrations, the activity of certain muscle enzymes (SDH and PFK) and muscle fibre composition were made on biopsy specimens from the gluteus medius muscle of 68 standardbred horses, ½ to 8 years old. The muscle fibres were classified in 3 major categories, slow twitch (ST), fast twitch and high oxidative (FTH) and fast twitch (FT) fibres. The percentage of FTH fibres was higher after the age of 4 years, averaging 54 %. ST fibres comprised 24 % and this...
A spin-label study of horse erythrocyte carbonic anhydrases C and D.
Comparative biochemistry and physiology. B, Comparative biochemistry    December 1, 1973   Volume 46, Issue 4 813-822 doi: 10.1016/0305-0491(73)90125-9
Chignell CF, Starkweather DK.No abstract available
Proceedings: Relation of cyclic AMP to sperm motility.
Journal of reproduction and fertility    December 1, 1973   Volume 35, Issue 3 591 doi: 10.1530/jrf.0.0350591
Tash J, Mann T.No abstract available
Activity of horse liver alcohol dehydrogenase SS with NADP (H) as coenzyme and its sensitivity to barbiturates.
Biochemical and biophysical research communications    October 1, 1973   Volume 54, Issue 3 1046-1052 doi: 10.1016/0006-291x(73)90799-7
Pietruszko R.No abstract available
A proteinase and proteinase inhibitor of mammalian sperm acrosomes.
Biology of reproduction    October 1, 1973   Volume 9, Issue 3 219-225 doi: 10.1093/biolreprod/9.3.219
Zaneveld LJ, Polakoski KL, Williams WL.No abstract available
Studies on the substrate specificity of acylneuraminate cytidylyltransferase and sialytransferase of submandibular glands from cow, pig and horse.
Hoppe-Seyler's Zeitschrift fur physiologische Chemie    October 1, 1973   Volume 354, Issue 10-11 1405-1414 doi: 10.1515/bchm2.1973.354.2.1405
Schauer R, Wember M.No abstract available
[Purification and properties of L-cysteinsulfinic decarboxylase from horse kidneys].
Bollettino della Societa italiana di biologia sperimentale    July 15, 1973   Volume 49, Issue 11 679-685 
Federici G, Santoro L, Tomati U, Cannella C.No abstract available
[L-cysteinsulfinic decarboxylase and L-cysteic decarboxylase in the liver and kidney of mammals].
Bollettino della Societa italiana di biologia sperimentale    July 15, 1973   Volume 49, Issue 11 675-678 
Federici G, Tomati U, Santoro L, Cannella C.No abstract available
The equilibrium unfolding parameters of horse and sperm whale myoglobin. Effects of guanidine hydrochloride, urea, and acid.
The Journal of biological chemistry    July 10, 1973   Volume 248, Issue 13 4623-4634 
Puett D.No abstract available
Small intestinal beta-galactosidase activity in the horse.
Gut    July 1, 1973   Volume 14, Issue 7 535-540 doi: 10.1136/gut.14.7.535
Roberts MC, Kidder DE, Hill FW.Two enzymes having lactase activity are present in the equine small intestine. The first, the digestive enzyme, neutral beta-galactosidase, declines in activity from birth to three years, disappearing completely between 3 and 4 years of age. The other, the soluble lysosomal enzyme, acid beta-galactosidase, having affinity for lactose and a synthetic beta-galactoside, shows a decrease in activity in the first three months of life and thereafter varies little in activity and represents the lactase enzyme in the adult horse. This pattern may parallel the development of lactase activity in many ot...
Reduction of ferricytochrome c by dithionite ion: electron transfer by parallel adjacent and remote pathways.
Proceedings of the National Academy of Sciences of the United States of America    June 1, 1973   Volume 70, Issue 6 1701-1703 doi: 10.1073/pnas.70.6.1701
Creutz C, Sutin N.The kinetics of the reduction of horseheart ferricytochrome c by sodium dithionite (phosphate buffer-sodium chloride; pH 6.5, mu = 1.0, 25 degrees ) features two reaction pathways; one with the rate constant k(3) = 1.17 x 10(4) M(-1) sec(-1), the other with the rate constant k(1)k(2)/k(-1) = 6.0 x 10(4) M(-1) sec(-1). These pathways are interpreted in terms of remote attack (possibly by way of the exposed edge of the porphyrin system) and adjacent attack (requiring the opening of the heme crevice). The limiting rate for the adjacent pathway (k(1) = 30 sec(-1)) is in good agreement with the rat...
Intra-species variation in chlorpromazine metabolism.
Research communications in chemical pathology and pharmacology    May 1, 1973   Volume 5, Issue 3 741-758 
Brookes LG, Forrest IS.No abstract available
Physical properties and subunit structure of butyrylcholinesterase from horse serum.
Biochemistry    April 10, 1973   Volume 12, Issue 8 1622-1630 doi: 10.1021/bi00732a025
Lee JC, Harpst JA.No abstract available
Aromatic phosphoryl thiocholines. 3. The kinetics of inhibition of purified horse serum cholinesterase.
Arhiv za higijenu rada i toksikologiju    February 1, 1973   Volume 24, Issue 2 117-126 
Maksimović M, Cosić M, Binenfeld Z.No abstract available
Intermicrosomal distribution of aromatizing enzyme system in equine testicular tissue.
Acta endocrinologica    February 1, 1973   Volume 72, Issue 2 366-375 doi: 10.1530/acta.0.0720366
Oh R, Tamaoki BI.The microsomal fraction (10 000–105 000 × g precipitate) of equine testes was fractionated into the smooth- and the rough-surfaced microsomal subfractions by a sucrose density-gradient centrifugation in the presence of CsCl. The validity of this fractionating procedure was confirmed by electron microscopic examination and also by chemical analysis of the RNA contents in these subfractions. The aromatizing enzyme system (19-hydroxylase and aromatase) which was concentrated in the microsomal fractions among the organellae was found to be localized in the smoothsurfaced microsomal fraction. Th...
Pancreatic ribonuclease distribution and comparisons in mammals.
Nature: New biology    January 17, 1973   Volume 241, Issue 107 76-78 doi: 10.1038/newbio241076a0
Beintema JJ, Scheffer AJ, van Dijk H, Welling GW, Zwiers H.No abstract available
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