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.
Isolation of -1,4 leads to 1,4-glucosyltransferase from horse muscle.
Archivum immunologiae et therapiae experimentalis    January 1, 1972   Volume 20, Issue 5 755-761 
Hutny J, Dzongowska-Dzongu T.No abstract available
Mammalian acid glucoamylases. I. Purification of glucoamylase from skeletal muscle.
Archivum immunologiae et therapiae experimentalis    January 1, 1972   Volume 20, Issue 5 745-753 
Iwanowski H.No abstract available
[Lysyl-arylamidase activity in the blood serum of domestic animals].
Veterinarni medicina    January 1, 1972   Volume 17, Issue 9 561-568 
Molnárová M, Bartík M, Samo A.No abstract available
35 C1 NMR studies of the active site zinc of horse liver alcohol dehydrogenase.
Biochemical and biophysical research communications    December 17, 1971   Volume 45, Issue 6 1444-1450 doi: 10.1016/0006-291x(71)90182-3
Ward RL, Happe JA.No abstract available
The complete enzymic hydrolysis of horse muscle acyl phosphatase.
Life sciences. Pt. 2: Biochemistry, general and molecular biology    September 8, 1971   Volume 10, Issue 17 983-988 doi: 10.1016/0024-3205(71)90101-9
Ramponi G, Cappugi G, Treves C, Nassi P.No abstract available
[Combined inhibition of horse serum cholinesterase by diphenylphosphinic and diphenylthiophosphinic esters].
Doklady Akademii nauk SSSR    September 1, 1971   Volume 200, Issue 1 103-106 
Brestkin AP, Brik IL, Volkova RI, Godovikov NN, Gurdaliev KhKh.No abstract available
Phosphorus metabolism in ponies fed varying levels of phosphorus.
The Journal of nutrition    September 1, 1971   Volume 101, Issue 9 1257-1263 doi: 10.1093/jn/101.9.1257
Schryver HF, Hintz HF, Craig PH.No abstract available
The binding of carbon dioxide by horse haemoglobin.
The Biochemical journal    August 1, 1971   Volume 124, Issue 1 31-45 doi: 10.1042/bj1240031
Kilmartin JV, Rossi-Bernardi L.1. Three modified horse haemoglobins have been prepared: (i) alpha(c) (2)beta(c) (2), in which both the alpha-amino groups of the alpha- and beta-chains have reacted with cyanate, (ii) alpha(c) (2)beta(2), in which the alpha-amino groups of the alpha-chains have reacted with cyanate, and (iii) alpha(2)beta(c) (2), in which the two alpha-amino groups of the beta-chain have reacted with cyanate. 2. The values of n (the Hill constant) for alpha(c) (2)beta(c) (2), alpha(2)beta(c) (2) and alpha(c) (2)beta(2) were (respectively) 2.5, 2.0 and 2.6, indicating the presence of co-operative interactions ...
Acid phosphatase activity in mouse brain infected with Venezuelan equine encephalomyelitis virus.
Journal of virology    August 1, 1971   Volume 8, Issue 2 232-241 doi: 10.1128/JVI.8.2.232-241.1971
Garcia-Tamayo J.The mode of development of Venezuelan equine encephalomyelitis virus and the activity of acid phosphatase in the central nervous system of newborn mice were investigated. Precursor particles appeared to be formed in masses of viroplasm, migrating to the membrane of the Golgi cisterns and vacuoles or to the plasma membrane and being transformed into mature viral particles by budding. Mature viral particles were also found in the lumen of the blood vessels and around the myelin sheath of axons. Increased number of Golgi complexes and depletion of polysomes were the main ultrastructural alteratio...
Purification and properties of butyrylcholinesterase from horse serum.
Archives of biochemistry and biophysics    July 1, 1971   Volume 145, Issue 1 55-63 doi: 10.1016/0003-9861(71)90009-9
Lee JC, Harpst JA.No abstract available
Limited proteolysis of horse heart cytochrome c.
European journal of biochemistry    June 11, 1971   Volume 20, Issue 3 414-419 doi: 10.1111/j.1432-1033.1971.tb01407.x
Schejter A, Goldkorn T, Sokolovsky M.No abstract available
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
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