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.
On the electron-transfer-coupled proton release of cytochrome c.
Biochimica et biophysica acta    April 6, 1971   Volume 234, Issue 1 57-61 doi: 10.1016/0005-2728(71)90129-0
Czerlinski GH, Dar K.No abstract available
Thermal stability of horse liver alcohol dehydrogenase and its complexes.
Archives of biochemistry and biophysics    April 1, 1971   Volume 143, Issue 2 354-358 doi: 10.1016/0003-9861(71)90221-9
Theorell H, Tatemoto K.No abstract available
[Enzyme diagnostics in horses].
Nordisk veterinaermedicin    January 1, 1971   Volume 23, Issue 1 23-34 
Edqvist LE, Ekman L, Persson S.No abstract available
[Purification, various properties and specificity of equine urinary kallikrein].
Anais da Academia Brasileira de Ciencias    December 31, 1970   Volume 42, Issue 4 773-781 
Prado JL, Prado ES, Stella RC, Webster ME.No abstract available
[Therapeutic action of a Catalase extracted from horse’s liver in the treatment of arthroses].
Rhumatologie    December 1, 1970   Volume 22, Issue 10 407-416 
Le Chevallier PL.No abstract available
Cholinesterase bonded to paper.
Canadian journal of biochemistry    December 1, 1970   Volume 48, Issue 12 1314-1317 doi: 10.1139/o70-204
Stasiw RO, Brown HD, Hasselberger FX.No abstract available
Ontogenetic variation of serum esterases in the horse.
Zentralblatt fur Veterinarmedizin. Reihe A    September 1, 1970   Volume 17, Issue 8 719-725 doi: 10.1111/j.1439-0442.1970.tb01052.x
Kaminski M, Podliachouk L, Vandeplassche M, Girard O.No abstract available
Serum esterases of Equidae: truly or apparently negative phenotypes.
Comparative biochemistry and physiology    September 1, 1970   Volume 36, Issue 1 207-209 doi: 10.1016/0010-406x(70)90668-7
Kaminski M, Podliachouk L.No abstract available
Methanol activity o alcohol dehydrogenases from human liver, horse liver, and yeast.
Archives of biochemistry and biophysics    September 1, 1970   Volume 140, Issue 1 52-59 doi: 10.1016/0003-9861(70)90009-3
Mani JC, Pietruszko R, Theorell H.No abstract available
Alkaline phosphatase in healing of wounds of skin and subcutis in the horse.
American journal of veterinary research    August 1, 1970   Volume 31, Issue 8 1389-1392 
Patel MR, Hardenbrook HJ.No abstract available
Horse liver alcohol dehydrogenase. The primary structure of an N-terminal part of the protein chain of the ethanol-active isoenzyme.
European journal of biochemistry    July 1, 1970   Volume 14, Issue 3 521-534 doi: 10.1111/j.1432-1033.1970.tb00319.x
Jörnvall H.No abstract available
[Enzymatic studies of serum in horses, cattle and dogs: glutamate dehydrogenase (GLDH), transaminases (GOT and GPT), lactate dehydrogenase (LDH) and sorbit dehydrogenase (SDH)].
Berliner und Munchener tierarztliche Wochenschrift    June 1, 1970   Volume 83, Issue 11 221-222 
Möhler C.No abstract available
Kinins released from horse heat-acid-denaturated plasma by plasmin, plasma kallikrein, trypsin and Bothrops kininogenase.
Biochemical pharmacology    June 1, 1970   Volume 19, Issue 6 2091-2096 doi: 10.1016/0006-2952(70)90307-2
Gapanhuk E, Henriques OB.No abstract available
Comparative action of various kininogenases on crude horse plasma substrates.
Biochemical pharmacology    June 1, 1970   Volume 19, Issue 6 2083-2090 doi: 10.1016/0006-2952(70)90306-0
Budnitskaya P, Gapanhuk E, Henriques OB.The kininogenase activity of trypsin, plasmin, plasma kallikrein and heated Bothrops venom was compared, using fresh, heated and heat-acid-denatured horse plasma as source of kininogen. The venom kininogenase was found to have the highest activity on fresh horse plasma, followed by plasmin and trypsin which were equally active, and plasma kallikrein which was half as active as plasmin on these substrates. Plasmin and trypsin released more kinin from heat-treated than from fresh plasma whereas kallikrein released half as much as it liberates from fresh plasma. On heat-aciddenatured plasma equal...
[Enzyme histochemical findings in the ultimobranchial body of the horse].
Endokrinologie    April 1, 1970   Volume 56, Issue 1 92-96 
Rother P.No abstract available
Differences in E and S chains from isoenzymes of horse liver alcohol dehydrogenase.
Nature    March 21, 1970   Volume 225, Issue 5238 1133-1134 doi: 10.1038/2251133a0
Jörnvall H.No abstract available
[Blood esterases in twin horses].
Comptes rendus des seances de la Societe de biologie et de ses filiales    January 1, 1970   Volume 164, Issue 3 538-540 
Kaminski M.No abstract available
[The genetics of 6-PGD (EC 1.1.1.44) in various mammals. II. Studies on four ungulata species. Isoenzyme polymorphisms in horse and swine].
Humangenetik    January 1, 1970   Volume 11, Issue 1 59-61 doi: 10.1007/BF00296304
Bender K, Hof JO, Engel W.No abstract available
Studies on the structure of ferritin and apoferritin from horse spleen. I. Tryptic digestion of ferritin and apoferritin.
Biochimica et biophysica acta    November 11, 1969   Volume 194, Issue 1 34-42 doi: 10.1016/0005-2795(69)90176-7
Crichton RR.No abstract available
Interaction of coenzyme with differently prepared zinc-free (apo) horse liver alcohol dehydrogenases.
The Journal of biological chemistry    November 10, 1969   Volume 244, Issue 21 5967-5971 
Hoagstrom CW, Iweibo I, Weiner H.No abstract available
Heterogeneity of erythrocyte catalase. Correlations between sulfhydryl group content, chromatographic and electrophoretic properties.
European journal of biochemistry    November 1, 1969   Volume 11, Issue 1 49-57 doi: 10.1111/j.1432-1033.1969.tb00737.x
Mörikofer-Zwez S, Cantz M, Kaufmann H, von Wartburg JP, Aebi H.No abstract available
Studies on equine trypsinogen and trypsin.
The Biochemical journal    October 1, 1969   Volume 114, Issue 4 82P doi: 10.1042/bj1140082pa
Harris CI, Hofmann T.No abstract available
The transport of oxidized glutathione from the erythrocytes of various species in the presence of chromate.
The Biochemical journal    October 1, 1969   Volume 114, Issue 4 833-837 doi: 10.1042/bj1140833
Srivastava SK, Beutler E.1. Erythrocytes from normal and glucose 6-phosphate dehydrogenase-deficient humans were subjected to hydrogen peroxide diffusion to oxidize the GSH. Studies were carried out in the presence and absence of chromate to inhibit glutathione reductase and with or without the addition of glucose. 2. The GSH content of erythrocytes from other species was oxidized by subjecting them to hydrogen peroxide diffusion in the presence of chromate and glucose. 3. Chromate (1.3mm) inhibited glutathione reductase by about 80%, whereas glucose 6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, hexokin...
Zinc isotope exchange in horse liver alcohol dehydrogenase.
Biochemistry    September 1, 1969   Volume 8, Issue 9 3792-3797 doi: 10.1021/bi00837a045
Drum DE, Li TK, Vallee BL.No abstract available
Stability studies on crude and purified horse serum cholinesterase.
Biochemical pharmacology    July 1, 1969   Volume 18, Issue 7 1701-1705 doi: 10.1016/0006-2952(69)90159-2
Beckett AH, Vaughan CL, Mitchard M.No abstract available
New sialic acid-containing sulfolipid: “ungulic acid”.
Journal of lipid research    July 1, 1969   Volume 10, Issue 4 440-444 
Leikola E, Nieminen E, Teppo AM.Human epidermis, hair, nails, and kidney as well as bovine and horses' hooves were found to contain a lipid fraction, which on thin-layer chromatography migrated slightly ahead of the cerebroside sulfate esters and gave the color reaction specific for sialic acid. This fraction was isolated from horse hoof, in which it constituted nearly half of the total lipids. The purified fraction contained sulfur, but no phosphorus. The IR spectrum revealed the presence of a sulfate group, which was also determined by the benzidine method. Thin-layer and gas-liquid chromatography of the products of acid h...
Lack of alpha-amylase in horse serum.
Experientia    June 15, 1969   Volume 25, Issue 6 597-598 doi: 10.1007/BF01896533
Franzini C, Bonini PA.No abstract available
The enzyme histochemistry of developing odontoblasts in cattle, pigs and horses.
The Histochemical journal    May 1, 1969   Volume 1, Issue 4 281-294 doi: 10.1007/BF01003275
Mori M, Sakiyama Y.The histochemical distribution of some hydrolytic and oxidative enzymes in developing odontoblasts and subodontoblasts in cattle, pigs and horses has been observed in cryostat sections of teeth that have been decalcified with neutral EDTA. Undifferentiated dental epithelium and immature odontoblasts of the bell stage tooth germ showed lower levels of enzymatic activity as compared with the well-developed tooth germ. When the dentine matrix began to form, the young odontoblasts appeared to have a significantly positive reaction for acid phosphatase, and gradually other enzymes developed a...
Enzymes of equine erythrocytes: changes during equine infectious anemia.
American journal of veterinary research    April 1, 1969   Volume 30, Issue 4 543-549 
Kaneko JJ, Tanaka S, Nakajima H, Ushimi C.No abstract available
[Chromogenic substrates of choline esterase from the blood serum of horses].
Biokhimiia (Moscow, Russia)    March 1, 1969   Volume 34, Issue 2 277-281 
Brestkin AP, Kats RI, Rozengart LA, Rozengart EV, Soboleva IN, Sokolovskiĭ MA.No abstract available
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