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 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
[The presence of plasminogen activator in kidney perfusate].
Przeglad lekarski    January 1, 1973   Volume 30, Issue 6 504-509 
Zuch A, Januszko T, Buluk K, Bielecki T.No abstract available
[Study of the mechanism of inhibition of horse liver alcohol dehydrogenase by 3, 5, 3′-triiodo-L-thyronine and its formic, acetic and propionic analogues].
Comptes rendus des seances de la Societe de biologie et de ses filiales    January 1, 1973   Volume 167, Issue 5 662-667 
Truchot R, Goudonnet H, Michel R.No abstract available
[Enzyme studies in the serum of large animals with reference to diagnosis and prognosis].
Tierarztliche Praxis    January 1, 1973   Volume 1, Issue 1 5-18 
Gerber H, Martig J, Straub R.No abstract available
Enzyme changes in ageing mammals.
Gerontologia    January 1, 1973   Volume 19, Issue 2 79-125 doi: 10.1159/000211964
Wilson PD.No abstract available
Species specificity in the isozyme spectrum of the alkaline phosphatase in bull, ram, stallion, boar and cock spermatozoa.
Comptes rendus de l'Academie Bulgare des sciences : sciences mathematiques et naturelles    January 1, 1973   Volume 26, Issue 11 1553-1555 
Petkov ZZ, Ivanov IN, Kichev GK.No abstract available
[Isolation of soluble isoltyrosinases extracted from horse melanoma].
Comptes rendus des seances de la Societe de biologie et de ses filiales    January 1, 1973   Volume 167, Issue 1 87-89 
Kleisbauer JP, Profisi-Centa G, Roubin R.No abstract available
[Laboratory diagnosis of liver diseases in the horse (1)].
Tierarztliche Praxis    January 1, 1973   Volume 1, Issue 2 177-186 
Sova Zd.No abstract available
Bilirubin uridyldiphospho-glucuronyl transferase and -glucuronidase activity in tissues of horse (Equus caballus) and sheep (Ovis aries).
Comparative biochemistry and physiology. B, Comparative biochemistry    December 15, 1972   Volume 43, Issue 4 929-933 doi: 10.1016/0305-0491(72)90236-2
Anwer MS, Mia AS, Gronwall R.No abstract available
Subcellular distribution of cyclic AMP-dependent protein phosphotransferases in horse thyroid gland.
Archives internationales de physiologie et de biochimie    December 1, 1972   Volume 80, Issue 5 984-985 
Sand G, Verhaegen M.No abstract available
Kininase activity in equine plasma.
Biochemical pharmacology    November 15, 1972   Volume 21, Issue 22 3078-3082 doi: 10.1016/0006-2952(72)90202-x
O-Ishi S, Sakuma A, Katori M.No abstract available
An examination of the oxidation of aldehydes by horse liver alcohol dehydrogenase.
The Journal of biological chemistry    November 10, 1972   Volume 247, Issue 21 7106-7107 
Hinson JA, Neal RA.No abstract available
Mechanisms of the reactions of cytochrome c. Rate and equilibrium constants for ligand binding to horse heart ferricytochrome c.
The Journal of biological chemistry    November 10, 1972   Volume 247, Issue 21 6932-6936 
Sutin N, Yandell JK.No abstract available
Glutathione reduction and other enzyme activities in equine erythrocytes.
Comparative biochemistry and physiology. B, Comparative biochemistry    October 15, 1972   Volume 43, Issue 2 413-417 doi: 10.1016/0305-0491(72)90301-x
Smith JE, Kiefer S, Lee M.1. Reduced glutathione regeneration rates as measured in erythro- cytes of ten horses were considerably lower than rates reported in human and sheep erythrocytes. 2. Theactivityofenzymesinvolvedinreducedglutathioneregenerationwas at least three times the observed reduction rate. 3. Despitehighglucose-6-phosphatedehydrogenaseactivity,equineerythro- cytes could not adequately accelerate the hexose monophosphate pathway. 4. Activities of enzymes involved in regulating the glycolytie pathway were less than 5/~moles/min per g hemoglobin; of other glycolytic enzymes greater than 10/~moles/min per...
Erythrocytic methaemoglobin reductases of various mammalian species.
Experientia    October 15, 1972   Volume 28, Issue 10 1248-1249 doi: 10.1007/BF01946202
Agar NS, Harley JD.No abstract available
Purification and some molecular properties of horse liver acyl phosphatase.
Biochimica et biophysica acta    October 12, 1972   Volume 284, Issue 2 485-496 doi: 10.1016/0005-2744(72)90147-7
Ramponi G, Nassi P, Cappugi G, Treves C, Manao G.No abstract available
Changes in cholinesterase activity in stored equine blood samples.
American journal of veterinary research    September 1, 1972   Volume 33, Issue 9 1893-1894 
Schindler RL, Kruckenberg SM.No abstract available
[Training effects on thoroughbreds. I. Muscle specific enzymes].
Zentralblatt fur Veterinarmedizin. Reihe A    July 1, 1972   Volume 19, Issue 7 537-545 
Riethmüller H, Wels A.No abstract available
Isolation and partial characterization of mare milk lysozyme.
Archives of biochemistry and biophysics    July 1, 1972   Volume 151, Issue 1 353-355 doi: 10.1016/0003-9861(72)90507-3
Jauregui-Adell J, Cladel G, Ferraz-Pina C, Rech J.No abstract available
Mechanistic studies on horse liver alcohol dehydrogenase. The influence of the different premixings on the transient kinetics of aldehyde reductions.
Biochemistry    June 6, 1972   Volume 11, Issue 12 2303-2310 doi: 10.1021/bi00762a015
Luisi PL, Favilla R.No abstract available
Imidazole: an inhibitor of L-phenylalanine-insensitive alkaline phosphatases of tissues other than intestine and placenta.
Biochimica et biophysica acta    May 12, 1972   Volume 268, Issue 2 415-421 doi: 10.1016/0005-2744(72)90337-3
Brunel C, Cathala G.1. Alkaline phosphatases (orthophosphoric monoester phosphohydrolase, EC 3.1.3.1) from brain, kidney, liver, bone, lung and spleen, which are not very sensitive to l-phenylalanine, are strongly inhibited by imidazole, whereas the placental and intestinal enzymes, which are very sensitive to l-phenylalanine, are only slightly affected. This is a new possibility for distinguishing the alkaline phosphatase isoenzymes. 2. The inhibition is apparently of an uncompetitive type, suggesting that the inhibitor interacts with the ES complex to form an EIS complex. 3. Histidine acts upon all enzyme...
Biochemical and electrophoretic studies of -galactosidase in normal man, in patients with Fabry’s disease, and in Equidae.
American journal of human genetics    May 1, 1972   Volume 24, Issue 3 237-249 
Beutler E, Kuhl W.No abstract available
[Heterogenity of arylamidases cleaving L-leucyl-p-nitroanilide in the blood serum of farm animals].
Veterinarni medicina    April 1, 1972   Volume 17, Issue 4 243-247 
Samo A, Bartík M.No abstract available
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