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.
[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
Horse muscle acyl phosphatase: purification and some properties.
Archives of biochemistry and biophysics    March 1, 1969   Volume 130, Issue 1 362-369 doi: 10.1016/0003-9861(69)90045-9
Ramponi G, Guerritore A, Treves C, Nassi P, Baccari V.No abstract available
The effect of chloroform on the liver and the activity of serum enzymes in the horse.
The Journal of pathology    February 1, 1969   Volume 97, Issue 2 241-251 doi: 10.1002/path.1710970209
Thorpe E, Gopinath C, Jones RS, Ford EJ.No abstract available
Common and species-specific serum esterases of Equidae. I. Horse and donkey.
Biochimica et biophysica acta    January 1, 1969   Volume 191, Issue 3 611-620 doi: 10.1016/0005-2744(69)90354-4
Kaminski M.No abstract available
[Occurrence of various enzymes in synovial fluid and tendon sheaths of horses].
Archiv fur experimentelle Veterinarmedizin    January 1, 1969   Volume 23, Issue 2 451-454 
Grün E, Panndorf H.No abstract available
Cleavage of horse immunoglobulin by cyanogen bromide.
Immunochemistry    November 1, 1968   Volume 5, Issue 6 513-524 doi: 10.1016/0019-2791(68)90088-8
Ernst ML, Arnon R, Sela M.No abstract available
Succinylcholine analogs as substrates and inhibitors of pseudocholinesterase.
Journal of medicinal chemistry    November 1, 1968   Volume 11, Issue 6 1126-1128 doi: 10.1021/jm00312a005
Beckett AH, Vaughan CL, Mitchard M.No abstract available
Action of horse urinary kallikrein on synthetic derivatives of bradykinin.
Biochemical pharmacology    October 1, 1968   Volume 17, Issue 10 2232-2234 doi: 10.1016/0006-2952(68)90200-1
Babel I, Stella RC, Prado ES.Previous experiments indicated that horse urinary kallikrein (UK) hydrolyzes salminei- e and polyarginine, a but not polylysine. This paper reports the action of UK on bradykinyl-serine, methionyllysyl-bradykinin and lysyllysyl-bradykinin.
A comparative study of vertebrate esterase multiplicity.
Comparative biochemistry and physiology    September 1, 1968   Volume 26, Issue 3 837-852 doi: 10.1016/0010-406x(68)90004-2
Holmes RS, Masters CJ, Webb EC.No abstract available
Inhibition of the pseudocholinesterase in horse serum by some choline analogues.
Biochemical pharmacology    August 1, 1968   Volume 17, Issue 8 1595-1599 doi: 10.1016/0006-2952(68)90220-7
Beckett AH, Vaughan CL, Mitchard M.No abstract available
Trehalase and maltase in the serum of vertebrates.
Comparative biochemistry and physiology    August 1, 1968   Volume 26, Issue 2 561-566 doi: 10.1016/0010-406x(68)90649-x
Van Handel E.No abstract available
The synthesis of some analogues of butyrylcholine and their hydrolysis by a purified horse serum cholinesterase.
Biochemical pharmacology    August 1, 1968   Volume 17, Issue 8 1591-1594 doi: 10.1016/0006-2952(68)90219-0
Beckett AH, Vaughan CL, Mitchard M.No abstract available