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.
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
Iodination of horse liver alcohol dehydrogenase.
Biochemical and biophysical research communications    March 10, 1972   Volume 46, Issue 5 1951-1955 doi: 10.1016/0006-291x(72)90075-7
Jörnvall H, Zeppezauer M.No abstract available
Structure of horse-muscle phosphoglycerate kinase at 6 angstrom resolution.
Nature: New biology    February 16, 1972   Volume 235, Issue 59 195-198 doi: 10.1038/newbio235195a0
Blake CC, Evans PR, Scopes RK.The single peptide chain of 3-phosphoglycerate kinase is folded into two distinct globular units, only one of which seems to be involved in substrate binding.
Innervation of sweat glands in horses and dogs.
The British journal of dermatology    February 1, 1972   Volume 86, Issue 2 160-163 doi: 10.1111/j.1365-2133.1972.tb16080.x
Bell M, Montagna W.The sweat glands in the digital pads of dogs are surrounded by nerves that are clearly demonstrated with techniques for acetyl‐ and butyryl‐cholinesterase. The glands in the hairy skin have no such nerves. In the horse, despite some variation in the abundance of demonstrable nerves around the glands, the latter are surrounded by nerves that are demonstrated only with techniques for acetylcholinesterase.
Purification of horse serum cholinesterase by preparative polyacrylamide gel electrophoresis.
The Journal of biological chemistry    January 25, 1972   Volume 247, Issue 2 566-571 
Main AR, Tarkan E, Aull JL, Soucie WG.No abstract available
Electronic, hydrophobic, and steric effects of binding of inhibitors to the horse liver alcohol dehydrogenase-reduced pyridine coenzyme binary complex.
Biochemistry    January 18, 1972   Volume 11, Issue 2 170-179 doi: 10.1021/bi00752a006
Sarma RH, Woronick CL.No abstract available
Effects of intraarticular flumethasone suspension on synovial effusion enzyme activity of arthritic horses.
Journal of the American Veterinary Medical Association    January 15, 1972   Volume 160, Issue 2 186-190 
Van Pelt RW, Tillotson PJ, Gertsen KE, Gallagher KF.No abstract available
[Effect of various surgico-orthopedic diaseases on the activity of the enzymes GOT, GPT, SODH and AP in the blood serum of horses].
Veterinarni medicina    January 1, 1972   Volume 17, Issue 6 359-366 
Tkác J, Sutta J.No abstract available
Cytoplasmic carboxylesterases of human and domestic animal liver: aggregation, dissociation, and molecular weight estimation.
Canadian journal of biochemistry    January 1, 1972   Volume 50, Issue 1 9-15 doi: 10.1139/o72-002
Ecobichon DJ.No abstract available
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
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