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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.
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...
Amino acid sequence of phospholipase A2 from horse pancreas.
The Journal of biological chemistry    February 25, 1977   Volume 252, Issue 4 1189-1196 
Evenberg A, Meyer H, Gaastra W, Verheij HM, De Haas GH.The complete amino acid sequence of phosphlipase A2 (EC 3.1.1.4) from horse pancreas was determined. The protein controls of a single polypeptide chain of 125 amino acids and has a molecular weight of 13,927. The chain is crosslinked by seven disulfide bridges. The sequence was determined by automated Edman degradation of the intact protein and several of the large peptide fragments. Smaller peptides were analyzed by manual Edman degradation. Fragmentation of the peptide chain was accomplished by enzymatic digestion with trypsin, chymotrypsin, and thermolysin. The final overlap was found by di...
Steady state kinetics and binding of eukaryotic cytochromes c with yeast cytochrome c peroxidase.
The Journal of biological chemistry    February 10, 1977   Volume 252, Issue 3 919-926 
Kang CH, Ferguson-Miller S, Margoliash E.1. The steady state kinetics for the oxidation of ferrocytochrome c by yeast cytochrome c peroxidase are biphasic under most conditions. The same biphasic kinetics were observed for yeast iso-1, yeast iso-2, horse, tuna, and cicada cytochromes c. On changing ionic strength, buffer anions, and pH, the apparent Km values for the initial phase (Km1) varied relatively little while the corresponding apparent maximal velocities varied over a much larger range. 2. The highest apparent Vmax1 for horse cytochrome c is attained at relatively low pH (congruent to 6.0) and low ionic strength (congruent to...
Transmission of the cytochrome c structural gene in horse-donkey crosses.
The Journal of biological chemistry    February 10, 1977   Volume 252, Issue 3 830-834 
Walasek OF, Margoliash E.Donkey cytochrome c was shown to differ from horse cytochrome c by having a serine in position 47 rather than a threonine. The rest of the amino acid sequences are identical. Mules and hinnies, both males and females, carry equal amounts of horse and donkey cytochromes c. The same ratio is found in hinnies in preparations from heart tissue and from skeletal muscle. These results demonstrate that cytochrome c is transmitted in horse-donkey crosses as a simple Mendelian character which is neither sex-linked nor shows dominance. The cytochrome c gene is therefore located in the nuclear genome, as...
Guanidination of horse methemoglobin.
Archives of biochemistry and biophysics    February 1, 1977   Volume 179, Issue 1 322-327 doi: 10.1016/0003-9861(77)90117-5
Sakura JD, Rupley JA.Reaction of horse methemoglobin with O-methylisourea at pH 10.2 results in 95% conversion of lysine residues to homoarginine. Analysis of the chymotryptic peptides showed that no single ϵ-amino group was unreactive. Guanidination decreases the dependence of the sedimentation coefficient on hydrogen ion concentration in the range of pH 8 to 11 and did not affect the dependence on protein concentration at pH 7. These results support the conclusion that the lysine side chains involved in subunit contacts have sufficient freedom to accommodate the small changes in bulk and geometry associated wit...
[Mechanisms for the expression of parental alleles of the Gpd locus in mule erythrocytes].
Genetika    January 1, 1977   Volume 13, Issue 10 1761-1766 
Serov OL, Zakiian SM, Kulichkov VA.No abstract available
Purification and characterization of equine herpesvirus-induced DNA.
Virology    January 1, 1977   Volume 76, Issue 1 395-408 doi: 10.1016/0042-6822(77)90311-7
Allen GP, O'Callaghan DJ, Randall CC.Infection of cells with equine herpesvirus type 1 (EHV-1) or type 3 (EHV-3) resulted in the induction of a DNA polymerase activity distinguishable from host cell DNA polymerases by its high salt requirement for maximal activity. By column chromatography on DEAE-cellulose, DNA-cellulose, phosphocellulose, and hydroxyapatite, the EHV-1-induced polymerase was purified 500-fold with 1–2% recovery of total activity from the nuclei of infected hamster livers. The final enzyme preparation was homogeneous as judged by electrophoresis in sodium dodecyl sulfate-polyacrylamide gels. Calculations based ...
Studies on cytochrome c. XIV. Synthesis of the protected heptadecapeptide (sequence 88-104) of horse heart cytochrome c.
International journal of peptide and protein research    January 1, 1977   Volume 10, Issue 2 95-101 
Borin G, Filippi B, Cavaggion F, Marchiori F.A solution synthesis is described of the partially protected N alpha-benzyloxycarbonylheptadecapeptide Z-Lys (Tfa)-Thr-Glu-Arg-Glu-Asp-Leu-Ile-Ala-Tyr-Leu-Lys (Tfa)-Lys (Tfa)-Ala-Thr-Asn-Glu (OBu t)-OBu t corresponding to sequence 88-104 of horse heart cytochrome c. The synthesis is achieved through the preparation of two subunits H1 (sequence 88-96) and H2 (sequence 97-104) and their linkage by an azide coupling step.
Cross-reactivity in the radioimmunoassay of ferritin with cells from high- and low-responder mice.
Biochemical Society transactions    January 1, 1977   Volume 5, Issue 1 256-258 doi: 10.1042/bst0050256
Deacon NJ, Ebringer A.No abstract available
Studies on cytochrome C. XIII. Synthesis of the protected undecapeptide (sequence 77-87) of horse heart cytochrome c.
International journal of peptide and protein research    January 1, 1977   Volume 10, Issue 2 89-94 
Borin G, Filippi B, Stivanello D, Marchiori F.A solution synthesis of Z-Gly-Thr-Lys (Tfa)-Met-Ile-Phe-Ala-Gly-Ile-Lys (Tfa)-Lys (Tfa)-NHNH-Boc corresponding to the sequence 77-87 of horse heart cytochrome c is described. The protected undecapeptide was obtained from intermediate hepta- and tetrapeptide fragments by an azide coupling.
Labeling of antilactose antibody.
Methods in enzymology    January 1, 1977   Volume 46 516-523 doi: 10.1016/s0076-6879(77)46062-2
Gopalakrishnan PV, Zimmerman UJ, Karush F.Affinity labeling studies with anticarbohydrate antibodies have been very limited. In earlier studies, diazoniumphenyl glycosides were employed as affinity labeling reagents for rabbit and equine anti-p-azophenyl-β-lactoside and p-azophenyl- β-galactoside antibodies. Although these antibodies were heterogeneous, it was possible to identify the labeled residues in the heavy or light chains since the modified residues had characteristic absorption spectra. With the discovery of bacterial cell walls of Streptococcus groups A and C induced antipolysaccharide antibodies of restricted heterogeneit...