Analyze Diet

Topic:Biochemistry

The study of biochemistry in horses encompasses the chemical processes and substances that occur within equine organisms. This field investigates the molecular interactions and pathways that are fundamental to horse physiology, including metabolism, enzyme activity, and genetic expression. Key areas of interest include the examination of metabolic disorders, nutrient absorption, and the biochemical basis of muscle function and energy production. Researchers utilize biochemical analysis to understand health and disease mechanisms in horses, contributing to the development of diagnostic tools and therapeutic strategies. This page gathers peer-reviewed studies and scholarly articles that explore various biochemical processes and their implications for equine health and performance.
Enzymes in organic synthesis. Influence of substrate structure on rates of horse liver alcohol dehydrogenase-catalysed oxidoreductions.
Journal of the Chemical Society. Perkin transactions 1    January 1, 1978   Volume 12 1636-1642 doi: 10.1039/p19780001636
Irwin AJ, Lok KP, Huang KW, Jones JB.No abstract available
Characterization and chemical modification of isolated allergens from horse hair and dandruff.
International archives of allergy and applied immunology    January 1, 1978   Volume 57, Issue 4 349-357 doi: 10.1159/000232124
Løwenstein H.No abstract available
Isoelectric focusing of horse serum esterase isozymes and detection of new phenotypes.
Animal blood groups and biochemical genetics    January 1, 1978   Volume 9, Issue 4 207-213 doi: 10.1111/j.1365-2052.1978.tb01438.x
Fisher RA, Scott AM.A new method for separating the isozymes of horse serum esterase is described. The improved resolution has enabled us to detect several previously undescribed phenotypes. This method has also been used to detect two different apparently 'silent' alleles.
Horse pancreatic colipase: isolation by a detergent method and amino terminal sequence of the polypeptide chain.
Biochimie    January 1, 1978   Volume 60, Issue 1 103-107 doi: 10.1016/s0300-9084(78)80207-7
Julien R, Rathelot J, Canioni P, Sarda L, Gregoire J, Rochat H.No abstract available
Common and species-specific esterases of Equidae–IV. Horse of przewalski, onager and Zebra hartmannae.
Comparative biochemistry and physiology. B, Comparative biochemistry    January 1, 1978   Volume 61, Issue 3 357-364 doi: 10.1016/0305-0491(78)90137-2
Kaminski M, Metenier L, Sykiotis M, Ryder OA, Demontoy MC.1. Among several species of Equidae only E. przewalskii possesses a serum esterase identical with that of E. caballus. 2. The esterases of Hemionidae differ slightly from that of domestic horse by electrophoretic migration and by antigenic structure. 3. Zebras (grevyi, burchelli) appear devoid of this component but Z. hartmannae possesses an esterase of high enzymatic activity, differing notably from that of horse by electrophoretic and antigenic properties.
The ‘normal range’ and precision of phytohaemagglutinin-induced equine lymphocyte transformation in vitro.
Research in veterinary science    January 1, 1978   Volume 24, Issue 1 87-91 
Dixon JB, Allan D, West CR.Data are presented on lymphocyte transformation by phytohaemagglutinin in 20 normal horses. The logarithms of transformation ratios were found to have an approximately normal distribution, giving (for the transformation ratios themselves) a geometric mean of 23.6, a range of 1.92 to 97.3, and an estimated 95 per cent tolerance interval of 1.1 to 488. Analysis of variance on the logarithms of the transformation ratios gave a coefficient of variation of 140 per cent of the transformation ratios themselves for the variation between horses; whereas the coefficient of variation between duplicate sa...
Comparative studies on blood serum alpha-L-fucosidases from several mammalian species.
Comparative biochemistry and physiology. B, Comparative biochemistry    January 1, 1978   Volume 60, Issue 4 459-461 doi: 10.1016/0305-0491(78)90077-9
Villar E, Calvo P, Cabezas JA.1. Peripheral blood serum alpha-L-fucosidases have been studied from various mammalian species: Sus scropha var domestica L. (pig), Capra hircus L. (goat), Bos taurus L. (bull, races Morucha and Charolais), Equus caballus L. (horse) and Equus asinus L. (donkey). 2. Fluorimetric and spectrophotometric procedures were used for determination of alpha-L-fucosidases. 3. alpha-L-Fucosidases were more active towards fluorescent substrates than towards chromogenic substrates. 4. pH optima values of the enzymes are: (A) 5.5 for sera from all above-mentioned species when fluorescent substrates were empl...
Polymorphic post-albumin of cattle and horse plasma identified as vitamin D binding protein (Gc protein).
Animal blood groups and biochemical genetics    January 1, 1978   Volume 9, Issue 1 37-40 doi: 10.1111/j.1365-2052.1978.tb01409.x
Gahne B, Juneja RK.Cattle and horse plasma samples of known post-albumin types were radiolabelled with 14C-vitamin D3. These samples were then analysed by polyacrylamide gel electrophoresis, followed by autoradiography. The patterns observed were identical to those of post-albumin variants. The polymorphic post-albumin protein of cattle and horse was thus identified as the vitamin D binding protein and homologous to the Gc protein of human plasma.
Genetic polymorphism of the vitamin D binding protein and another post-albumin protein in horse serum.
Animal blood groups and biochemical genetics    January 1, 1978   Volume 9, Issue 1 29-36 doi: 10.1111/j.1365-2052.1978.tb01408.x
Juneja RK, Gahne B, Sandberg K.Horizontal polyacrylamide gel electrophoreses, on 10% separation gel, of horse serum revealed polymorphism of the vitamin D binding protein (Gc protein) and another post-albumin protein (Pa). Family data supported the hypothesis that Gc and Pa types were controlled by autosomal codominant alleles. For both Gc and Pa proteins, the homozygous types showed a single fraction while the heterozygous type had two fractions. Pa types were found to be identical to the post-albumin types reported earlier by starch gel electrophoresis. Two Gc alleles, GcF and GcS, and three Pa alleles, Pa D, Pa F and Pa ...
The null allele in the horse esterase (Es) system detected by enzyme assay and rocket immunoelectrophoresis in heterozygous animals.
Animal blood groups and biochemical genetics    January 1, 1978   Volume 9, Issue 4 197-205 doi: 10.1111/j.1365-2052.1978.tb01437.x
Kaminski M.The detection of the recessive null allele of horse serum esterase (Es) is possible in heterozygotes Es+/EsO which by starch gel electrophoresis appear like homozygotes Es+/Es+. Two methods are proposed, the titration of enzymatic activity of esterase and the immunochemical titration of esterase as antigen. These methods can be applied to solve the cases of suspect parentage or in population studies.
The influence of neuroleptanalgesia on the serum activity of muscle enzymes in ponies.
Equine veterinary journal    January 1, 1978   Volume 10, Issue 1 60-64 doi: 10.1111/j.2042-3306.1978.tb02217.x
Hillidge CJ.The serum activities of creatine kinase (CPK), aldolase (ALD) and alpha-hydroxybutyrate dehydrogenase (HBD) were determined in a group of Welsh Mountain ponies before and after a 30 minute period of neuroleptanalgesia induced by i.v. injection of Immobilon and terminated by i.v. injection of Revivon. There were slight but significant increases in the serum activities of CPK and HBD following neuroleptanalgesia, but no change in the serum activity of ALD. It is suggested that this form of neuroleptanalgesia may be associated, in ponies, with a degree of reversible myocardial hypoxic change, pos...
Regulation of the synthesis of M protein by sugars, Todd Hewitt broth, and horse serum, in growing cells of Streptococcus pyogenes.
Microbios    January 1, 1978   Volume 21, Issue 85-86 185-212 
Pine L, Reeves MW.Various sugars were tested for their effect on the differential rate of synthesis of M protein during the growth of Streptococcus pyogenes strain 0055 M12T12. In a semisynthetic medium alone, a high rate of M protein synthesis occurred with glucose as a substrate; decreasing rates of synthesis occurred with sucrose and trehalose, in that order, although the rates of growth were approximately equal with all sugars. A period of derepressed synthesis of M protein occurred in the lag phase of growth and in the stationary period as the substrates were being depleted. Although glucose inhibited the ...
Analysis of a complex antigenic site on horse cytochrome c.
Advances in experimental medicine and biology    January 1, 1978   Volume 98 119-129 doi: 10.1007/978-1-4615-8858-0_6
Jemmerson R, Margoliash E.Of the antigenic determinants so far identified for cytochrome c, only one involves more than a single amino acid substitution between the immunogen and host proteins. Both a threonine at position 89 and a glutamic acid at position 92 control one of the three antigenic sites identified in horse cytochrome c, as expressed in rabbits. Three antibody subpopulations, all directed against this region of the molecule, were isolated from the serum of a single rabbit by adsorption on a series of insolubilized cytochromes c. Antibody fluorescence quenching titrations with a variety of cytochromes c wer...
Activity of adenosine deaminase and purine nucleoside phosphorylase in erythrocytes and lymphocytes of man, horse and cattle.
Comparative biochemistry and physiology. B, Comparative biochemistry    January 1, 1978   Volume 61, Issue 3 439-441 doi: 10.1016/0305-0491(78)90151-7
Tax WJ, Veerkamp JH.1. Activities of ADA and PNP were measured in erythrocytes and lymphocytes of man, horse and cattle. 2. In bovine hemolysates both enzyme activities are low when compared with activities in human hemolysates. In horse hemolysates both enzyme activities are virtually absent. 3. Enzyme activities are consistently lower (about 50%) in intact lymphocytes than in sonicated lymphocytes. This finding suggests that the uptake of nucleosides is rate-limiting for both enzymes in intact lymphocytes. 4. The activity of ADA in horse lymphocytes is comparable to that in lymphocytes of patients with severe c...
Somatostatin-containing cells in the rat and horse pancreatic islets.
The Tohoku journal of experimental medicine    January 1, 1978   Volume 124, Issue 1 57-64 doi: 10.1620/tjem.124.57
Ito S, Yamada Y, Hayashi M, Matsubara Y.Somatostatin-, glucagon- and insulin-containing cells in the rat and horse pancreatic islets were investigated by an indirect immunofluorescent technique using antibodies to insulin, glucagon and somatostatin. In the rat pancreatic islets, insulin-containing cells were located centrally, and glucagon and somatostatin or somatostatin-like substance (SLS)-containing cells were peripherally disposed and glucagon-containing cells were situated more peripherally as compared with distribution of somatostatin-containing cells. On the other hand, in the horse pancreatic islets, insulin-containing cell...
Comparative warfarin binding to albumin from various species.
Biochemical pharmacology    December 15, 1977   Volume 26, Issue 24 2445-2447 doi: 10.1016/0006-2952(77)90455-5
Seller EM, Lang-Sellers ML, Koch-Weser J.No abstract available
Interrelationship of Na, HCO3, and volatile fatty acid transport by equine large intestine.
The American journal of physiology    December 1, 1977   Volume 233, Issue 6 E469-E478 doi: 10.1152/ajpendo.1977.233.6.E469
Argenzio RA, Southworth M, Lowe JE, Stevens CE.No abstract available
Ultrastructural observations suggesting merocrine secretion in the initial segment of the mammalian epididymis.
Cell and tissue research    November 23, 1977   Volume 184, Issue 4 487-490 doi: 10.1007/BF00220971
Nicander L, Malmqvist M.Principal cells in the initial segment of the epididymis in horses, cattle, pigs, sheep, dogs, cats, and rabbits have an abundant, partly rough, endoplasmic reticulum and a large Golgi complex. Small vacuoles with opaque content seem to be formed by the Golgi complex and move to the cell apex, where they empty their contents into the lumen by a merocrine mechanism.
Thymidine concentrations in serum and urine of different animal species and man.
Biochemical pharmacology    November 15, 1977   Volume 26, Issue 22 2175-2179 doi: 10.1016/0006-2952(77)90271-4
Nottebrock H, Then R.No abstract available
Lactoperoxidase-catalyzed iodination of horse cytochrome c:monoiodotyrosyl 74 cytochrome c.
The Journal of biological chemistry    November 10, 1977   Volume 252, Issue 21 7743-7751 
Osheroff N, Feinberg BA, Margoliash E, Morrison M.Iodination of horse cytochrome c with the lactoperoxidase-hydrogen peroxide-iodide system results initially in the formation of the monoiodotyrosyl 74 derivative. This singly modified protein was obtained in pure form by ion exchange chromatography and preparative column electrophoresis. It shows an intact 695 nm absorption band, the midpoint potential of the native protein, a nuclear magnetic resonance spectrum which indicates an undisturbed heme crevice structure, a normal reaction with antibodies directed against native horse cytochrome c, and circular dichroic spectra in which the only cha...
IgM antibody–III. The role of light chains in equine anti-lactose Fabmu.
Immunochemistry    November 1, 1977   Volume 14, Issue 11-12 781-786 doi: 10.1016/0019-2791(77)90347-0
Mitchell KF, Karush F, Morgan DO.No abstract available
A subunit-sized butyrylcholinesterase present in high concentrations in pooled rabbit serum.
The Biochemical journal    November 1, 1977   Volume 167, Issue 2 367-376 doi: 10.1042/bj1670367
Main AR, McKnelly SC, Burgess-Miller SK.A butyrylcholinesterase of mol.wt. approx. 83000 was observed in pooled rabbit serum. The enzyme was named monomeric butyrylcholinesterase to distinguish it from the larger oligomeric butyrylcholinesterase of horse and human serum whose subunits are the same size as the monomeric enzyme. The active-site concentration of monomeric butyrylcholinesterase in the pooled serum was 0.18mum, which is five times the concentration of butyrylcholinesterase in pooled horse serum. This was surprising, since the horse serum is regarded as a rich source of butyrylcholinesterase, whereas rabbit serum is not g...
Studies related to the metabolism of anabolic steroids in the horse: 19-nortestosterone.
Xenobiotica; the fate of foreign compounds in biological systems    November 1, 1977   Volume 7, Issue 11 683-693 doi: 10.3109/00498257709038698
Houghton E.1. The metabolism of 19-nortestosterone in a cross-bred horse has been studied using 14C-labelled material. 2. Two neutral metabolites isolated from urinary extracts by column chromatography were identified as isomers of 3-hydroxyestran-17-one and estrane-3,17-diol by g.l.c.-mass spectrometry. 3. The stereochemistry of the two metabolites has been investigated by comparison of the retention times of their trimethylsilyl derivatives with those of standard steroids of known configuration.
Staining of glycosaminoglycans in intervertebral disc cells.
Research in veterinary science    November 1, 1977   Volume 23, Issue 3 351-355 
Butler WF, Pousty I.Disc material from horse, ox, sheep, pig, dog and cat was stained by the Alcian-blue-critical electrolyte concentration technique and with the standard and two-step periodic acid Schiff methods. The effects of pretreatment with hyaluronidase and with chondroitinase was also evaluated. There appears to be a small increase in total cellular glycosaminoglycan content with age in all species: cellular material of high molecular weight however only increases in aged animals. The degree of sulphation of cellular glycosaminoglycans does not vary with age or with position in the disc.
Circular dichroism of porcine, bovine, and equine pancreatic phospholipases A2 and their zymogens. Unusual conformations simulating helix content.
Biochimica et biophysica acta    October 26, 1977   Volume 494, Issue 2 285-292 doi: 10.1016/0005-2795(77)90157-x
Jirgensons B, de Haas GH.Conformation of porcine, bovine, and equine pancreatic phospholipases A2 (EC 3.1.1.4) and their zymogens was studied by the circular dichroism (CD) probe in the far and near ultraviolet spectral zones. All these phospholipases and their zymogens displayed CD curves suggesting the presence of moderate amounts of α-helical conformation. However, on the basis of known primary structure and recent X-ray structural analysis of prophospholipase A2 crystals (Drenth, J., Enzing, C.M., Kalk, K.H. and Vessies, J.C.A. (1976) Nature 264, 373–377), it has to be concluded that the positive CD band cen...
Studies on a number of erythrocytic enzymes and intermediate products of equine erythrocyte metabolism.
Tijdschrift voor diergeneeskunde    October 15, 1977   Volume 102, Issue 20 1197-1203 
Franken P, Schotman JH.The activities and concentrations of a number of erythrocytic enzymes and intermediate products of erythrocyte metabolism were determined in twenty-one normal standard-bred horses which were studied clinically and biochemically. These studies showed that equine anaerobic glycolysis is characterized by a biochemical pattern similar to that observed in human PK deficiency. The greater sensitivity of equine haemoglobin to oxidants is attributable either to low stability of GSH, which may be due either to the low activity of GR or that of 6PGD as observed in the studies. In addition, the saturatio...
Familial methaemoglobinaemia and haemolytic anaemia in the horse associated with decreased erythrocytic glutathione reductase and glutathione.
Equine veterinary journal    October 1, 1977   Volume 9, Issue 4 198-201 doi: 10.1111/j.2042-3306.1977.tb04029.x
Dixon PM, McPherson EA, Muir A.A trotter mare with a history of poor performance was found to have methaemoglobinaemia and haemolytic anaemia associated with decreased erythrocyte glutathione reductase and glutathione levels. The mare's dam, which also had a history of poor performance, was subsequently found to be similarly affected.
Analysis of normal equine serum using the SMA 12/60 Autoanalyzer.
Veterinary medicine, small animal clinician : VM, SAC    October 1, 1977   Volume 72, Issue 10 1629-1633 
Porter T, McCashin FB.No abstract available
Nucleolar fragmentation in cells infected with alphaviruses (39886).
Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine (New York, N.Y.)    October 1, 1977   Volume 156, Issue 1 109-112 doi: 10.3181/00379727-156-39886
Stanton GJ, Osborne LC, Albrecht TB.No abstract available
Semisynthetic cytochrome c.
Proceedings of the National Academy of Sciences of the United States of America    October 1, 1977   Volume 74, Issue 10 4248-4250 doi: 10.1073/pnas.74.10.4248
Barstow LE, Young RS, Yakali E, Sharp JJ, O'Brien JC, Berman PW, Harbury HA.Horse heart cytochrome c can be split with cyanogen bromide into a heme peptide (residues 1-65) and a nonheme peptide (residues 66-104). In a process involving (i) complex formation between the two fragments and (ii) restoration of the severed peptide linkage, a fully active cytochrome c preparation can be re-formed. Use has been made of this process to couple the heme peptide to peptide 66-104 synthesized by the Merrifield solid-phase procedure. The semisynthetic product formed in this manner is indistinguishable from reconstituted cytochrome c prepared with nonsynthetic peptide 66-104.