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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.
Conformation of immunoglobulin M. I. Characterization of anti-epsilon-1-dimethylamino-5-naphthalenesulfonyl-L-lysine immunoglobulin M antibodies from horse, pig, and shark.
Biochemistry    July 27, 1976   Volume 15, Issue 15 3373-3379 doi: 10.1021/bi00660a032
Holowka DA, Cathou RE.IgM antibodies specific for the fluorophore epsiolon-1-dimethylamino-5-naphthalenesulfonyl-L-lysine(DNS-lysine) were elicited in the horse and nurse shark by immunization with a DNS-lysine streptococcal conjugate; the antibodies were purified by specific adsorption with an immunoadsorbent followed by gel filtration to select the IgM class (molecular weight 900 000). About 90% of the equine anti-DNS was IgM.DNS-Lysine, when bound in the combining sites of a population of these anti-DNS IgM antigodies from horse and nurse shark, as well as from pig, exhibited a marked fluorescence enhancement an...
[Preparative isolation of alpha 2-macroglobulin, transferrin, albumin and study of their nonspecific gamma-inhibitory activity].
Voprosy virusologii    July 1, 1976   Issue 4 461-464 
Saiatov MKh, Beĭsembaeva RU.Profiles of distribution of non-specific gamma-inhibitors of influenza A2/Victoria/35/72 in donkey and horse sera were established by gel chromatography in Sephadex G-200. High and low molecular inhibitors were found in 19S and 4S serum fractions. Highly purified preparations of a2-macroglobulin, transferrine and albumin were isolated by a combination of methods of salt precipitation, gel chromatography on Sephadex G-100, G-200 and ion exchange on DEAE-Sephadex A-50. Heating sera resulted in a considerable increase of the antiviral activity of a2-macroglobulin and transferrine and a reduction ...
Crystalline 3-phospho-d-glycerate kinase from horse muscle.
Biochemistry    June 29, 1976   Volume 15, Issue 13 2899-2901 
Johnson PE, Maister SG, Knowles JR.Phosphoglycerate kinase has been isolated in crystalline form from horse muscle. A convenient isolation procedure is described that yields homogeneous enzyme of specific activity 700 units/mg (30 degrees C). The enzyme is monomeric, and has a molecular weight 47 000. Of the eight cysteine residues in the protein, two react rapidly with Nbs21 with the concomitant loss of the catalytic activity. Since the isolation of phosphoglycerate kinase from yeast (Bücher, 1955) there have been several reports of purification methods yielding enzyme approaching molecular homogeneity, from rabbit muscle (Be...
Letter: Kinetics of reduction of horse-heart ferricytochrome c by catechol.
Journal of the American Chemical Society    June 23, 1976   Volume 98, Issue 13 4023-4024 doi: 10.1021/ja00429a061
Toppen DL.No abstract available
A correction to the sequence of the alpha chains of horse haemoglobin.
Journal of molecular biology    May 25, 1976   Volume 103, Issue 3 675-677 doi: 10.1016/0022-2836(76)90227-8
Ladner R, Air GM, Fogg JH.No abstract available
Catalytic iodination of proteins by horse myeloperoxidase in solid state.
Analytical biochemistry    May 7, 1976   Volume 72 372-379 doi: 10.1016/0003-2697(76)90544-3
Dubin A, Silberring J.No abstract available
Chromosome banding: a modified method for consistent G-banding in cattle, horses and buffaloes.
The Veterinary record    May 1, 1976   Volume 98, Issue 18 358 doi: 10.1136/vr.98.18.358-a
Halnan CR.No abstract available
Kinetic studies of the oxidation and reduction of Chromatium high potential iron-sulfur protein (HiPIP) by inorganic complexes. Comparison of the electron transfer reactivities of HiPIP and horse heart cytochrome c.
Journal of the American Chemical Society    April 14, 1976   Volume 98, Issue 8 2177-2180 doi: 10.1021/ja00424a028
Rawlings J, Wherland S, Gray HB.No abstract available
Horse-liver alcohol dehydrogenase and Pseudomonas testosteroni 3(17)beta-hydroxysteroid dehydrogenase transfer epimeric hydrogens from NADH to 17beta-hydroxy-5alpha-androstan-3-one. An exception to one of the Alworth-Bentley rules.
European journal of biochemistry    April 1, 1976   Volume 63, Issue 2 427-429 doi: 10.1111/j.1432-1033.1976.tb10244.x
Groman EV, Schultz RM, Engel LL, Orr JC.In the reduction of 17beta-hydroxy-5alpha-androstan-3-one to the 3beta-alcohol, horse liver alcohol dehydrogenase utilizes the 4-pro-R hydrogen of NADH whereas the 3(17)beta-hydroxysteroid dehydrogenase of Pseudomonas testosteroni utulized the 4-pro-S hydrogen. These observations provide an exception to the rule proposed by Alworth and Bentley that with regard to the paired methylene hydrogens at C-4 of NADH and NADPH "the stereospecificity of a particular reaction is fixed and does not vary with the source of the enzyme preparation". It is also apparent that for these two enzymes, the selecti...
Three-dimensional structure of horse liver alcohol dehydrogenase at 2-4 A resolution.
Journal of molecular biology    March 25, 1976   Volume 102, Issue 1 27-59 doi: 10.1016/0022-2836(76)90072-3
Eklund H, Nordström B, Zeppezauer E, Söderlund G, Ohlsson I, Boiwe T, Söderberg BO, Tapia O, Brändén CI, Akeson A.No abstract available
Characterization of protein phosphokinase activities in horse thyroid nuclei.
Biochimica et biophysica acta    March 11, 1976   Volume 429, Issue 1 163-172 doi: 10.1016/0005-2744(76)90038-3
Verhaegen M, Sand G.The distribution of protein phosphokinase (EC 2.7.1.37) activities has been established in horse thyroid nuclei. The presence of several enzyme activities has been demonstrated, two of which are clearly distinct. The first one acts on histone as substrate and is activated by cyclic AMP. Physico-chemical properties of this nuclear cyclic AMP-dependent histone kinase and of the cytosol histone kinase are different, demonstrating the absence of a contamination from the cytosol. The second enzyme acts on casein as substrate and is not stimulated by cyclic AMP POR CYCLIC GMP. The findings are consi...
Inactivation of horse liver alcohol dehydrogenase by modification of cysteine residue 174 with diazonium-1H-tetrazole.
Biochemistry    March 9, 1976   Volume 15, Issue 5 1087-1093 doi: 10.1021/bi00650a021
Sogin DC, Plapp BV.Diazonium-1H-tetrazole was tested as a potential active-site-directed reagent for amino acid residues involved in catalysis by alcohol dehydrogenase. In a novel reaction with a protein, diazonium-1H-tetrazole inactivated the enzyme selectively, and almost stoichiometrically, but reacting with the sulfur of a cysteine residue, Cys-174. As a model compound, the tetrazole adduct of free cysteine was prepared. Elementary and spectral analyses of the adduct were consistent with the structure 5-tetrazoleazo-S-cysteine. The adduct absorbs light with a maximun at 316 nm, and is destroyed by irradiatio...
Isolation and some molecular parameters of elastase-like normal proteinases from horse blood leucocytes.
The Biochemical journal    February 1, 1976   Volume 153, Issue 2 389-396 doi: 10.1042/bj1530389
Dubin A, Koj A, Chudzik J.Cytoplasmic granules were isolated from horse blood polymorphonuclear leucocytes by the heparin method and extracted with 0.9% NaCl by repeated freezing. Soluble proteins were separated on a column of Sephadex G-75 followed by chromatography on a column of CM-Sephadex with a NaCl gradient. Gel filtration, density-gradient centrifugation, isoelectric focusing and 0.1% sodium dodecyl sulphate/polyacrylamide-gel electrophoresis at pH 7.0 and at pH 4.5 were used to determine molecular parameters of proteinases. Three enzymes hydrolysing both casein and N-benzyloxycarbonyl-L-alanine nitrophenyl est...
Cell-free synthesis of equine herpesvirus type 3 nucleocapsid polypeptides.
Virology    February 1, 1976   Volume 69, Issue 2 751-762 doi: 10.1016/0042-6822(76)90503-1
Allen GP, Bryans JT.No abstract available
Immunochemical studies on blood groups. Immunochemical properties of B-active and non-B-active blood group substances from horse gastric mucosae and the relative size distributions of oligosaccharides liberated by base-borohydride.
Archives of biochemistry and biophysics    February 1, 1976   Volume 172, Issue 2 524-534 doi: 10.1016/0003-9861(76)90105-3
Newman W, Kabat EA.No abstract available
Primary structure determination of two cytochromes c2: close similarity to functionally unrelated mitochondrial cytochrome C.
Proceedings of the National Academy of Sciences of the United States of America    February 1, 1976   Volume 73, Issue 2 472-475 doi: 10.1073/pnas.73.2.472
Ambler RP, Meyer TE, Kamen MD.The amino-acid sequences of the cytochromes c2 from the photosynthetic non-sulfur purple bacteria Rhodomicrobium vannielii and Rhodopseudomonas viridis have been determined. Only a single residue deletion (at position 11 in horse cytochrome c) is necessary to align the sequences with those of mitochondrial cytochromes c. The overall sequence similarity between these cytochromes c2 and mitochondrial cytochromes c is closer than that between mitochondrial cytochromes c and the other cytochromes c2 of known sequence, and in the latter multiple insertions and deletions must be postulated before a ...
Characterization of human, bovine, and horse antithrombin III.
Biochemistry    January 27, 1976   Volume 15, Issue 2 368-373 doi: 10.1021/bi00647a020
Kurachi K, Schmer G, Hermodson MA, Teller DC, Davie EW.A comparison of the physical-chemical properties of human, bovine, and horse antithrombin III has been made. These three plasma proteins are strong inhibitors of bovine factor Xa and form a 1:1 molar complex with this coagulation enzyme. Human, bovine, and horse antithrombin III are glycoproteins containing hexose, hexosamine, and neuraminic acid. The total carbohydrate was 9, 12, and 16% for human, bovine, and horse antithrombin III, respectively. These proteins have a similar amino acid composition, although some monor variations were noted. Each antithrombin III is composed of a single poly...
Chemical modification as a probe of the topography and reactivity of horse-spleen apoferritin.
European journal of biochemistry    January 15, 1976   Volume 61, Issue 2 545-550 doi: 10.1111/j.1432-1033.1976.tb10049.x
Wetz K, Crichton RR.In apoferritin, but not in ferritin, 1.0 +/- 0.1 cysteine residue per subunit can be modified. In ferritin 3.3 +/- 0.3 lysine residues and 7.1 +/- 0.7 carboxyl groups per subunit can be modified, whilst the corresponding values for apoferritin are 4.4 +/- 0.4 lysine residues and 11.0 +/- 0.4 carboxyl groups per subunit. Modification of lysine residues which maleic anhydride and carboxyl groups with glycineamide in apoferritin which has been dissociated and denatured in guanidine hydrochloride leads to the introduction of 9.1 +/- 0.5 maleyl groups per subunit and 22.0 +/- 0.9 glycineamide resid...
Ligand binding properties of horse hemoglobins containing deutero- and mesoheme.
The Journal of biological chemistry    January 10, 1976   Volume 251, Issue 1 45-52 
Seybert DW, Moffat K, Gibson QH.The reactions of horse globin reconstituted with proto-, deutero-, and mesoheme have been examined by equilibrium and kinetic methods. In virtually all reactions studied, mesohemoglobin displays the more extreme functional behavior, whereas deuterohemoglobin exhibits behavior which is either very similar to native hemoglobin or intermediate between the two. Our kinetic and equilibrium results indicate that the primary effect of heme modification on the functional properties of hemoglobin is to alter the intrinsic reactivities of the deoxy and liganded conformations. Heme modification does not,...
Purification, characterization, and quantitation of the antigen employed in the immunodiffusion test for diagnosis of equine infectious anemia.
Preparative biochemistry    January 1, 1976   Volume 6, Issue 2-3 193-211 doi: 10.1080/00327487608061612
Hart LT, Braymer HD, Larson AD, Broussard EA.Equine infectious anemia (EIA) antigen extracted from the spleen of horses infected with EIA virus was purified by pH treatment, (NH4)2SO4 fractionation and affinity chromatography. The homogeneity of the antigen was indicated by sedimentation rate and sedimentation equilibrium experiments. A S20,w of 0.51 was determined and a molecular weight of 7600 was calculated from sedimentation equilibrium analysis. The amino acid composition of the pure antigen indicated the antigen is an acidic protein. Employing radical immunodiffusion (RID) and pure antigen a method for quantitating antigen content ...
Isolation and partial characterization of three major allergens of horse hair and dandruff.
International archives of allergy and applied immunology    January 1, 1976   Volume 51, Issue 1 48-67 doi: 10.1159/000231578
Løowenstein H, Markussen B, Weeke B.Three major allergens of horse hair and dandruff have been isolated. The fractionation procedures involved various combinations, described in detail, of ethanol precipitation below --5degreesC, cation- and anion-exchange chromatography, and gel filtration. UV absorption, quantitative immunoelectrophoresis and RAST inhibition were used to monitor the separations. Protein impurities constituted less than 5% in all cases. The molecular weights of the isolated proteins were 1.9 X 10(4), 5.1 X 10(4) and 3.1 X 10(4) daltons, respectively. The pIs were determined as 4.1, 3.8 and 3.9, respectively. Th...
Comparative studies of human, equine, porcine and bovine erythrocyte membrane sialoglycoproteins.
Comparative biochemistry and physiology. B, Comparative biochemistry    January 1, 1976   Volume 55, Issue 1 37-44 doi: 10.1016/0305-0491(76)90169-3
Hamazaki H, Hotta K, Konishi K.No abstract available
Acid phosphatase heterogeneity in horse neutrophil and eosinophil leukocytes.
Enzyme    January 1, 1976   Volume 21, Issue 6 540-552 doi: 10.1159/000458906
Heyneman RA, Bruyninckx WJ, Vercauteren RE.Two distinct groups of acid phosphatase containing granules were characterized in neutrophils, each group displaying different multiple forms of the enzyme. The heavy granule acid phosphatase showed a lysosomal location. A second lighter group of particles contained a thermolabile, thiol-dependent acid p-nitrophenyl and alpha-naphtylphosphatase, an enzyme clearly different from lysosomal acid phosphatase. Acid phosphatase activity from eosinophil leukocytes appeared to be totally associated with the typical eosinophil granules. On mechanical disruption of these particles, an acid phosphatase w...
Primary structure of equine growth hormone.
International journal of peptide and protein research    January 1, 1976   Volume 8, Issue 5 435-444 doi: 10.1111/j.1399-3011.1976.tb02523.x
Zakin MM, Poskus E, Langton AA, Ferrara P, Santomé JA, Dellacha JM, Paladini AC.No abstract available
Muscle structure and function–an explanation.
Equine veterinary journal    January 1, 1976   Volume 8, Issue 1 17-19 doi: 10.1111/j.2042-3306.1976.tb03276.x
Stewart M.The structure of vertebrate skeletal muscle is reviewed. The mechanism of muscular contraction and its control is then discussed from the point of view of molecular structure. Contraction takes place by a sliding filament mechanism produced by cross-bridges which form between thick and thin filaments. Control is exercised by tropomyosin and troponin. When the calcium concentration is low, these proteins interfere with the formation of cross-bridges and prevent contraction, but when the calcium concentration is increased, they no longer interfere and contraction proceeds.
N-acetylserine in horse muscle acylphosphatase.
International journal of peptide and protein research    January 1, 1976   Volume 8, Issue 3 269-273 
Cappugi G, Chellini PC, Nassi P, Ramponi G.A ninhydrin-negative peptide fraction obtained from tryptic digest of carboxymethyl acylphosphatase was isolated by chromatography on a column of PA 28 Beckman resin and analysed for the amino acid composition. Degradation with carboxypeptidase B and A indicated that the sequence of this peptide was: X-Thr-Ala-Arg. The amino-terminal residue was identified as N-acetylserine by high voltage electrophoresis. It is therefore suggested that the sequence of the NH2-terminal portion of CM-acylphosphatase is N-acetyl-Ser-Thr-Ala-Arg. Digestion with carboxypeptidase A and B indicated also that the COO...
Carbohydrate composition of horse spleen ferritin.
Biochimica et biophysica acta    November 10, 1975   Volume 411, Issue 1 165-167 doi: 10.1016/0304-4165(75)90295-0
Shinjyo S, Abe H, Masuda M.The carbohydrate composition of horse spleen ferritin was studied. 1 mol of the apoferritin, the protein moiety of ferritin, contains 25 mol of hexose, 3 mol of hexosamine and 10 mol of fucose. Same carbohydrate composition was detected in the apoferritin from iron rich ferritins. These results indicate that horse spleen ferritin is composed of non-identical subunits as regards its carbohydrate composition.
Conjugate paralogous crossing-over as an explanation for the tyrosine/phenylalanine polymorphism at position 24 in both alpha-chains of horse hemoglobin.
Journal of molecular evolution    November 4, 1975   Volume 6, Issue 3 233-236 doi: 10.1007/BF01732359
Beintema JJ.No abstract available
Oxygen affinity responses to 2,3-diphosphoglycerate, and methaemoglobin formation in horse and human haemoglobins.
Research in veterinary science    November 1, 1975   Volume 19, Issue 3 259-262 
McLean JG, Lewis IM.The oxygen affinities of horse and human haemoglobins were compared in the absence and presence of the allosteric effector 2,3-diphosphoglycerate (2,3-DPG). Horse haemoglobin solutions showed significantly smaller responses to the presence of 2,3-DPG, and this difference may be due to different amino acid substitutions at position NA2(2)beta. Horse haemoglobin solutions from erythrocytes containing different ratios of the two different haemoglobin types showed similar oxygen affinities in the absence and presence of 2,3-DPG. Horse haemoglobins in solution were found to autoxidise to methaemogl...
Isolation and partial characterization of the major glycoproteins of horse and swine erythrocyte membranes.
Biochimica et biophysica acta    October 6, 1975   Volume 406, Issue 2 206-213 doi: 10.1016/0005-2736(75)90005-x
Fujita S, Cleve H.The major glycoproteins of horse and swine erythrocyte membranes were isolated and examined chemically and immunologically. The major glycoprotein of horse erythrocyte membranes had a molecular weight of 33 000 and consisted of 46.2% protein and 53.8% carbohydrate, of which 9.4% was hexose, 10.1% hexosamine and 33.7% sialic acid. This glycoprotein was associated with activity for the infectious mononucleosis heterophile antigen. There were two different major glycoproteins in swine erythrocyte membranes. One major glycoprotein had a molecular weight of 46 200 and consisted of 34.2% protein and...