Analyze Diet

Topic:Molecular biology

Molecular biology in horses involves the study of molecular processes and genetic mechanisms that underpin equine physiology and health. This field encompasses the analysis of DNA, RNA, proteins, and other biomolecules to understand gene expression, genetic variation, and cellular functions in horses. Techniques such as genomic sequencing, gene expression profiling, and molecular diagnostics are employed to explore topics like hereditary diseases, performance traits, and immune responses in equines. This page assembles peer-reviewed research studies and scholarly articles that investigate the molecular biology of horses, focusing on genetic research, molecular techniques, and their applications in equine science.
The interaction of some bis-aryl compounds with sites of known structure of human and horse haemoglobin [proceedings].
British journal of pharmacology    March 1, 1978   Volume 62, Issue 3 428P-429P 
Goodford PJ.No abstract available
Circular dichroic properties and conformation of thionicotinamide dinucleotides bound to horse-liver alcohol dehydrogenase.
European journal of biochemistry    February 1, 1978   Volume 83, Issue 2 593-599 doi: 10.1111/j.1432-1033.1978.tb12128.x
Joppich-Kuhn R, Luisi PL.The interaction between horse liver alcohol dehydrogenase and the oxidized and reduced forms of the 3-thionicotinamide--adenine dinucleotide coenzyme analogues (sNAD and sNADH) has been investigated by ultraviolet absorption, fluorescence and circular dichroism. The fluorescence of sNADH is enhanced when bound to the enzyme, and the protein fluorescence is quenched by both sNADH (60--65%) and sNAD (65%). The possible origin of the larger quenching produced by sNAD with respect to that of NAD is discussed. Coenzyme dissociation constants have been determined by monitoring the quenching of the p...
Synthetic antigens. Horse “natural” antibodies against interpolymer of styrene and maleic acid (PSM).
Archivum immunologiae et therapiae experimentalis    January 1, 1978   Volume 26, Issue 1-6 67-71 
Ugorski M, Mikulska J, Skibiński G, Wieczorek Z, Lisowski J.Properties of horse natural anti-PSM antibodies are described. The antibodies were of IgG class. Electrostatic forces were mainly involved in reaction of PSM with horse antibodies. The reaction was inhibited by low molecular compounds resembling structural unit of PSM. Studies of difference spectra and ORD and CD spectra showed no major conformational changes in horse antibodies after reaction with PSM.
Stability and kinetic behavior of carboxymethylated horse muscle acylphosphatase.
Physiological chemistry and physics    January 1, 1978   Volume 10, Issue 4 367-373 
Stefani M, Berti A, Camici G, Manao G, Cappugi G, Ramponi G.Horse muscle acylphosphatase consists of a main chain S-S bound to glutathione. It was found that removal of the glutathione by reduction and successive carboxymethylation of the only cysteine of the main chain affects the stability of the enzyme, mainly with respect to thermal inactivation. On the other hand, the kinetic properties of the enzyme are affected very little.
Chromosome banding studies of the Equidae.
Cytogenetics and cell genetics    January 1, 1978   Volume 20, Issue 1-6 332-350 
Ryder OA, Epel NC, Benirschke K.No abstract available
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
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
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 ...
Replication of equine herpesvirus type 1 and type 3: resistance to hydroxyurea and thymidine.
Intervirology    January 1, 1978   Volume 9, Issue 5 276-285 doi: 10.1159/000148945
Allen GP, Cohen JC, Randall CC, O'Callaghan DJ.The replication of equine herpesvirus type 1 (EHV-1) and type 3 (EHV-3) was unimpeded in three different cell types-equine epithelial cells, equine fibroblasts, and mouse fibroblasts-which had been blocked in their capacity to synthesize host DNA by 2.5 mM hydroxyurea (HU) or 2 mM thymidine (TdR). The rate of DNA synthesis in uninfected or equine herpesvirus-infected cells in the presence of HU or TdR was measured by pulse-labeling cell samples with a labeled DNA precursor at different times after infection. DNA synthesis in uninfected cultures was completely inhibited by both compounds. Howev...
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...
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...
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...
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.
Phylogeny of the neurophysins: complete amino acid sequence of horse MSEL-neurophysin.
FEBS letters    August 15, 1977   Volume 80, Issue 2 374-376 doi: 10.1016/0014-5793(77)80479-1
Chauvet MT, Codogno P, Chauvet J, Acher R.No abstract available
The structure of horse methaemoglobin at 2-0 A resolution.
Journal of molecular biology    August 15, 1977   Volume 114, Issue 3 385-414 doi: 10.1016/0022-2836(77)90256-x
Ladner RC, Heidner EJ, Perutz MF.No abstract available
The oxidation of ferrocytochrome c in nonbinding buffer.
Canadian journal of biochemistry    August 1, 1977   Volume 55, Issue 8 796-803 doi: 10.1139/o77-118
Peterman BF, Morton RA.The apparent equilibrium constant and rate of oxidation was investigated for the reaction of cytochrome c with iron hexacyanide. It was found that if horse heart ferricytochrome c was exposed to ferricyanide (to oxidize traces of reduced protein) the cytochrome subsequently, even after extensive dialysis, had an apparent equilibrium constant different from that of electrodialyzed protein. The effect of ferricyanide ion apparently cannot be removed by ordinary dialysis. The ionic strength dependence of the apparent equilibrium constant and bimolecular oxidation rate constant was measured in the...
Electron-transfer protein reactivities. Kinetic studies of the oxidation of horse heart cytochrome c, Chromatium vinosum high potential iron-sulfur protein, Pseudomonas aeruginosa azurin, bean plastocyanin, and Rhus vernicifera stellacyanin by pentaamminepyridineruthenium(III).
Journal of the American Chemical Society    July 20, 1977   Volume 99, Issue 15 5158-5167 doi: 10.1021/ja00457a042
Cummins D, Gray HB.No abstract available
Electronic and steric factors affecting ligand binding: horse hemoglobins containing 2,4-dimethyldeuteroheme and 2,4-dibromodeuteroheme.
The Journal of biological chemistry    June 25, 1977   Volume 252, Issue 12 4225-4231 
Seybert DW, Moffat K, Gibson QH, Chang CK.Horse globin has been recombined with 2,4-dimethyldeuteroheme and 2,4-dibromodeuteroheme to yield the corresponding reconstituted hemoglobins, and the ligand binding reactions of these reconstituted hemoglobins have been examined in detail. Both hemoglobins exhibit relatively high n values, but 2,4-dimethyldeuterohemoglobin displays a consistently higher oxygen affinity than native hemoglobin, whereas the oxygen affinity of 2,4-dibromodeuterohemoglobin is consistently lower than that of native hemoglobin. The rate constants l’, and 1’4 for the binding of the first and fourth molecules of C...
Equine angiotensin converting enzyme: a zinc metalloenzyme.
Clinical and experimental pharmacology & physiology    May 1, 1977   Volume 4, Issue 3 267-281 doi: 10.1111/j.1440-1681.1977.tb02624.x
Fernley RT.1. Angiotensin I converting enzyme from horse plasma has been extensively purified and shown to be homogeneous by disc-gel electrophoresis. 2. The metal ion involved in the catalytic reaction of the enzyme has been identified for the first time as zinc by atomic absorption spectrometry. 3. A number of other physicochemical properties of the enzyme are described and compared with results obtained by other investigators. The molecular weight was determined by gel filtration to be 113 000 daltons. The pH maximum was found to be 7-4. The chloride activation of the enzyme appears to act by facilita...
Methods for quantifying mammalian spermatogenesis: a review.
Journal of animal science    May 1, 1977   Volume 44, Issue 5 818-833 doi: 10.2527/jas1977.445818x
Berndtson WE.No abstract available
RNA-dependent DNA polymerase associated with equine infectious anemia virus.
Journal of virology    April 1, 1977   Volume 22, Issue 1 16-22 doi: 10.1128/JVI.22.1.16-22.1977
Archer BG, Crawford TB, McGuire TC, Frazier ME.Equine infectious anemia (EIAV) is shown to have an associated RNA-instructed DNA polymerase similar in its cofactor requirements and reaction conditions to the RNA tumor virus DNA polymerases. Demonstrating this DNA polymerase activity requires a critical concentration of a nonionic detergent, all four deoxyribonucleoside triphosphates, and a divalent metal ion. The reaction is sensitive to RNase, and a substantial fraction of the FNA synthesized is complementary to viral RNA. The detection of a complex of tritium-labeled polymerase product DNA-template RNA, which sedimented at 60S to 70S, pr...
IgM antibody–I. Heterogeneity of the component chains of equine anti-lactose antibody.
Immunochemistry    March 1, 1977   Volume 14, Issue 3 161-164 doi: 10.1016/0019-2791(77)90189-6
Mitchell KF, Karush F, Morgan DO.The heterogeneity of the IgM response has been studied with anti-lactose antibody purified from the sera of seven horses. The IgM antibody was induced with a bacterial vaccine and the sera were obtained during a one-year period of immunization. L and H chain preparations were derived from separate bleedings of each horse and examined by analytical isoelectric focusing. All of the L chain preparations were complex and similar and, under optimum conditions, exhibited about 45 bands. Their similarity included almost identical concentration distributions over the entire pH gradient. Isoelectric ba...
Probing DNA quaternary ordering with circular dichroism spectroscopy: studies of equine sperm chromosomal fibers.
Biopolymers    March 1, 1977   Volume 16, Issue 3 573-582 doi: 10.1002/bip.1977.360160308
Sipski ML, Wagner TE.No abstract available
Prostaglandin F2alpha specific binding in equine corpora lutea.
Prostaglandins    March 1, 1977   Volume 13, Issue 3 553-564 doi: 10.1016/0090-6980(77)90032-6
Kimball FA, Wyngarden LJ.Preliminary studies indicate the presence of PGF2alpha specific binding sites in membrane fractions prepared from equine corpora lutea. The equilibrium binding data indicate an apparent dissociation constant of 3.2 X 10(-9)M and the concentration of binding sites of -0.1 pmoles/mg membrane protein. Competition of several natural prostaglandins for equine luteal PGF2alpha specific binding sites indicates specificity for the 9alpha-hydroxyl moiety and the 5,6-cis doublebond. Significant increases in relative binding affinities were demonstrated for PGF2alpha analogs with a phenyl ring introduced...