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.
[Different forms of cholinesterase in horse plasma]. Bajgar J.No abstract available
Comparative histochemical distribution of “leucine amino-peptidase” in the placenta and foetal membranes.
Histochemie. Histochemistry. Histochimie    January 1, 1967   Volume 10, Issue 3 272-277 doi: 10.1007/BF00304875
Christie GA.No abstract available
Attempts to demonstrate 3-beta- and 17-beta-hydroxy-steroid dehydrogenases histochemically in the testes of the stallion, boar, ram and bull.
Journal of reproduction and fertility    December 1, 1966   Volume 12, Issue 3 551-560 doi: 10.1530/jrf.0.0120551
Hay MF, Deane HW.No abstract available
Changes in the activity of proteolytic enzymes and transaminases (G.O.T., G.P.T.) in horse leucocytes during hyperimmunization.
Archives roumaines de pathologie experimentales et de microbiologie    December 1, 1966   Volume 25, Issue 4 971-978 
Ségli G, Toma E, Oprişan R.No abstract available
[On the behavior of serum transaminases in the trotting race horse after training].
Wiener tierarztliche Monatsschrift    February 1, 1966   Volume 53, Issue 2 95-107 
Ullrich W.No abstract available
[Activity determinations of serum enzymes in veterinary medicine. 3. F. LDH isoenzymes in various organs and the serum of diseases and healthy horses].
Schweizer Archiv fur Tierheilkunde    January 1, 1966   Volume 108, Issue 1 33-46 
Gerber H.No abstract available
[Serum enzyme activity determination in veterinary medicine. 3. Serum enzyme model in paralytic myoglobinemia of the horse].
Schweizer Archiv fur Tierheilkunde    December 1, 1965   Volume 107, Issue 12 685-697 
Gerber H.No abstract available
The reaction of organophosphorus compounds with hydrolytic enzymes. The inhibition of horse liver aliesterase.
Biochemical pharmacology    December 1, 1965   Volume 14, Issue 12 1727-1738 doi: 10.1016/0006-2952(65)90262-5
Ooms AJ, Breebaart-Hansen JC.No abstract available
[Determination of serum enzyme activities in veterinary medicine. 3. D. Determination of LDH, MDH, SHD, GLDH, ALD and alpha-amylase activity in some horse organs as a basis for the clinical interpretation of serum enzyme activity determinations].
Schweizer Archiv fur Tierheilkunde    November 1, 1965   Volume 107, Issue 11 626-631 
Gerber H.No abstract available
Proteolysis of salmine by horse urinary kallikrein.
Biochemical pharmacology    November 1, 1965   Volume 14, Issue 11 1665-1671 doi: 10.1016/0006-2952(65)90021-3
Brandi CM, Mendes J, Paiva AC, Prado ES.No abstract available
Cell and Solution Velocity Constants for the Reaction CO + Hb –> COHb at Different Temperatures in Mammals with Different Red Cell Sizes.
The Journal of general physiology    November 1, 1965   Volume 49, Issue 2 199-220 doi: 10.1085/jgp.49.2.199
Holland RA.Using a double beam stopped-flow apparatus, measurements were made of the velocity constant of the reaction CO + Hb --> COHb in solution and in the red cells of human beings, rabbits, horses, and goats. The solution constant (l') at 37 degrees C for human beings was 362 mM(-1) sec.(-1); in other species l' was somewhat lower. Two rabbits, despite having apparently identical hemoglobins had significantly different values for l'. The energy of activation (E) of l' was between 8 and 11 kcal/mole in all cases. The cell reaction constant (l'(c)) at 37 degrees was between 61 and 73 mM(-1) sec.(-1...
The action of cyanogen bromide on horse-heart cytochrome c and horse-heart myoglobin.
The Biochemical journal    September 1, 1965   Volume 96, Issue 3 693-699 doi: 10.1042/bj0960693
Black JA, Leaf G.1. The effects of cyanogen bromide on horse-heart cytochrome c and horse-heart myoglobin have been investigated. Cytochrome c yielded four fragments, of which two were haemopeptides. The two colourless peptides had amino acid compositions corresponding to those that are expected, on the basis of the sequence proposed for horse-heart cytochrome c by Margoliash, Smith, Kreil & Tuppy (1961), from cleavage at both methionine residues. Of the two haemopeptides, one was isolated and shown to be that derived from cleavage at only one methionine residue, that nearer to the C-terminus of the peptid...
Histochemistry of the equine lung: oxidative enzymes of the interalveolar septum.
American journal of veterinary research    July 1, 1965   Volume 26, Issue 113 960-964 
Tyler WS, Pearse AG, Rhatigan P.No abstract available
Sex-Linkage of Glucose-6-Phosphate Dehydrogenase in the Horse and Donkey.
Science (New York, N.Y.)    June 18, 1965   Volume 148, Issue 3677 1603-1604 doi: 10.1126/science.148.3677.1603
TRUJILLO JM, WALDEN B, O'NEIL P, ANSTALL HB.Distinctly different electrophoretic patterns of red cell glucose-6-phosphate dehydrogenase were resolved from the hemolyzates of horse and donkey erythrocytes. Examination of their reciprocal hybrids, mules and hinnies, showed that the red cells of female mules and female hinnies contain both horse and donkey G-6-PD; the male mule with an X chromosome from its horse mother contained pure horse G-6-PD, whereas the male hinny with the donkey X chromosome contained pure donkey G-6-PD. These findings on the male reciprocal hybrids suggest X-linkage.
Occurrence of cholinesterase isoenzymes in horse serum.
Nature    March 13, 1965   Volume 205, Issue 976 1110-1111 doi: 10.1038/2051110a0
Reiner E, Seuferth W, Hardegg W.No abstract available
[Alkylation of histidine radicals in the active center of horse myoglobin].
Bulletin de la Societe de chimie biologique    January 1, 1965   Volume 47, Issue 11 2178-2182 
Dautrevaux M, Han K, Boulanger Y, Biserte G.No abstract available
Comparative Studies on Plasma Enzyme Activities in Experimental Hepatic Necrosis in the Horse.
Research in veterinary science    January 1, 1965   Volume 6 18-23 
FREEDLAND RA, HJERPE CA, CORNELIUS CE.No abstract available
[On the mechanism of inhibition by choline of acetylcholine hydrolysis by horse serum cholinesterase].
Biokhimiia (Moscow, Russia)    January 1, 1965   Volume 30, Issue 1 137-140 
Brestkin AP, Ivanova LA, Svechnikova VV.No abstract available
Ions and the kininogenic activity of horse urinary kallikrein.
Acta physiologica latino americana    January 1, 1965   Volume 15, Issue 4 386-395 
Prado JL, Katchburian AV, Mendes J, Prado ES.No abstract available
STUDIES OF ESTERASES AND MULTIPLE FORMS OF CHOLINESTERASE IN EQUINE PLASMA.
Canadian journal of physiology and pharmacology    January 1, 1965   Volume 43 147-156 doi: 10.1139/y65-014
OKI Y, OLIVER WT, FUNNELL HS.No abstract available
Horse Heart Cytochrome C: Spectrophotometric Titration and Viscosity Changes in Alkaline Solution.
Biochemistry    November 1, 1964   Volume 3 1648-1650 doi: 10.1021/bi00899a008
RUPLEY JA.No abstract available
On the zinc content of horse liver alcohol dehydrogenase.
Biochemical and biophysical research communications    October 14, 1964   Volume 17, Issue 3 211-214 doi: 10.1016/0006-291x(64)90385-7
Akeson A.No abstract available
[Relationship between the potassium content of erythrocytes of some animal species and the sodium and potassium dependent adenosine triphosphatase activity of the red blood cells].
Archivio di scienze biologiche    October 1, 1964   Volume 48, Issue 4 409-415 
Lucaroni A, Millo A.No abstract available
Multiple Forms of Cholinesterase in Horse Plasma.
Nature    August 8, 1964   Volume 203 605-606 doi: 10.1038/203605a0
OKI Y, OLIVER WT, FUNNELL HS.No abstract available
An Attempt to Determine the Equilibrium Constant for the Reaction Between Acetylcholine and the Anionic Centers of Horse Plasma Cholinesterase.
International journal of neuropharmacology    July 1, 1964   Volume 3 333-339 doi: 10.1016/0028-3908(64)90026-7
ZUPANCIC AO.No abstract available
Hydrogen Transfer Between Reduced Diphosphopyridine Nucleotide Dehydrogenase and the Respiratory Chain. II. An Initial Lag in the Oxidation of Reduced Diphosphopyridine Nucleotide.
The Journal of biological chemistry    June 1, 1964   Volume 239 2049-2054 
MINAKAMI S, SCHINDLER FJ, ESTABROOK RW.No abstract available
Ceruloplasmins of Several Animal Species: Comparison of Electrophoretic Mobilities and Substrate Specificity. MARTIN GM, DERR MA, BENDITT EP.No abstract available
Comparative Examination of Carboxylic Esterases in Sera of Horse, Donkey, and Their Hybrids.
Nature    February 15, 1964   Volume 201 716-718 doi: 10.1038/201716a0
KAMINSKI M, GAJOS E.TWENTY-THREE fresh and 28 frozen (1–11 years old) samples of horse sera, 62 frozen donkey sera (3–11 years old), 24 frozen mule sera (2–10 years old), and 1 frozen 2-year-old serum sample of a hinny (offspring of a she-ass by a stallion) were studied by starch- and agar-gel electrophoresis (starch gel: horizontal migration, discontinued buffer system; tris-citrate pH 8.7 and borate 0.3 M, pH 8.2; 2 V/cm for 14 h; 10 samples analysed simultaneously; 0.1 ml. serum mixed with soluble starch Merck; agar gel: 0.8 per cent agar in veronal buffer 0.025 M, pH 8.2; 4.5 V/cm; 2½ h; 10 samples on ...
Acetylcholinesterase Activity in the Atrio-Ventricular Connections in Some Domestic Mammals.
Rivista di biologia    January 1, 1964   Volume 57 31-51 
CIAMPOLI A, PALMIERI G, ASOLE A.No abstract available
Biochemical and Histochemical Studies on 3-Beta-Hydroxysteroid Dehydrogenase Activity in the Adrenal Glands and Ovaries of Diverse Mammals.
Endocrinology    December 1, 1963   Volume 73 748-763 doi: 10.1210/endo-73-6-748
RUBIN BL, DEANE HW, HAMILTON JA.No abstract available