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.
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...
Digitoxin metabolism by rat liver microsomes.
Biochemical pharmacology    September 1, 1975   Volume 24, Issue 17 1639-1641 doi: 10.1016/b978-0-12-152810-2.50012-7
Schmoldt A, Benthe HF, Haberland G, Scott WA, Mahoney E, BOSE SK.No abstract available
Long chain base and fatty acid compositions of equine kidney sphingolipids.
Journal of biochemistry    September 1, 1975   Volume 78, Issue 3 527-536 doi: 10.1093/oxfordjournals.jbchem.a130937
Hara A, Taketomi T.Equine renal glycopshingolipids were composed of galactocerebroside, glucocerbroside, ceramide dihexoside, ceramide trihexoside, sulfatide, globoside I, Forssman globoside, and hematoside. Free ceramide and sphingomyelin were also found in equine kidney. Their long chain bases consisted of sphingosine, dihydrosphingosine, C18-phytosphingosine, and C20-phytosphingosine, whereas the fatty acids were separated into two groups: nonhydroxy and hydroxy fatty acids. Ceramide monohexoside was separated into five spots by TLC on borax-impregnated plates. The major component of ceramide monohexoside was...
Digitoxin metabolism by rat liver microsomes.
Biochemical pharmacology    September 1, 1975   Volume 24, Issue 17 1639-1641 doi: 10.1016/0005-7967(77)90095-x
Schmoldt A, Benthe HF, Haberland G, Sinelnikova EM, Dvoretskova TV, Kagan ZS, Marshall WL, Stoian M, Andrews WR.It has been shown that for the reaction catalyzed by "biodegradative" L-threonine dehydratase from E. coli strains K-12 and 980 in 0.5 M phosphate-carbonate buffer, pH 8.4 and pH 9.5, the plots of initial reaction rate (v) versus the initial substrate concentration ([S]0 are characterized by several inflection points, i. e. an intermediate plateau. The plot of v versus the allosteric activator (AMP) concentration have very complicated shapes: there are several inflection points, and also the maximum at L-threonine concentration equal to 3-10(2) and 5-10(-2) M. High AMP concentrations inhibit t...
Digitoxin metabolism by rat liver microsomes.
Biochemical pharmacology    September 1, 1975   Volume 24, Issue 17 1639-1641 doi: 10.1016/0006-291x(75)90200-4
Schmoldt A, Benthe HF, Haberland G, Jallon JM, Risler Y, Iwatsubo M, Karuzina II, Bachmanova GI, Kuznetsova GP, Izotov MV, Archakov AI, Kröger H....It has been found that NADPH-dependent hydroxylation of dimethylaniline, aniline, p- and o-nitroanisol and lipid peroxidation is inhibited by the tyrosine-copper (II) complex (low molecular weight analog of superoxide dismutase), which is indicative of a possibility of superoxide radicals formation in these reactions. The inhibition of the above-mentioned reactions with Tyr2-Cu2+ is less pronounced or absent, if cumole hydroperoxide is used as cosubstrate instead of NADPH. Differences in the Tyr2-Cu2+ complex effects on the cumule hydroperoxide-dependent xenobiotics hydroxylation and lipid per...
Immunological and chemical correlation between alpha-fetoproteins from human and several mammalian species.
Annals of the New York Academy of Sciences    August 22, 1975   Volume 259 109-118 doi: 10.1111/j.1749-6632.1975.tb25407.x
Nishi S, Watabe H, Hirai H.Alpha-Fetoproteins of several animals were purified and their molecular weights, amino acid compositions and peptide maps were compared, demonstrating the close similarities. These data indicated that the alpha-fetoproteins of mammalian species have closely related antigenical and chemical structures. Rabbits and horses were immunized with human alpha-fetoprotein, and it was observed that the animals produced antibodies reaction not only with human alpha-fetoprotein but with their homologous alpha-fetoproteins. The results were interpreted as the breakdown of the tolerance to their own alpha-f...
Conformational energy refinement of horse-heart ferricytochrome c.
Biochemistry    August 12, 1975   Volume 14, Issue 16 3509-3517 doi: 10.1021/bi00687a001
Warme PK, Scheraga HA.The reported X-ray structure of horse-heart ferricytochrome c has been refined by conformational energy calculations, using a three-stage computational procedure. In stage I, the atomic positions are adjusted to conform to idealized bond lengths and bond angles characteristic of small amino acid derivatives, while yet remaining as close as possible to the X-ray coordinates. In stage II, atomic overlaps are eliminated by adjusting the backbone and side-chain dihedral angles to minimize the nonbonded energy, hydrogen-bonded energy, and rotational energy contributions. In the final stage of refin...
The influence of amino acid substitutions on the conformational energy of cytochrome c.
Biochemistry    August 12, 1975   Volume 14, Issue 16 3518-3526 doi: 10.1021/bi00687a002
Warme PK.Conformational energies have been evaluated for each of the staggered side-chain conformations associated with the 261 amino acid substitutions known to occur among 60 eucaryotic species. At least 86% of these substitutions can be sterically accommodated (one at a time) within the structure of horse-heart cytochrome c resulting from conformational energy refinement. Simultaneous incorporation of all pertinent amino acid substitutions found in eight representative species into the refined horse-heart structure is also shown to be sterically possible, with few exceptions. In two cases (Pekin duc...
Differences in subunit composition and iron content of isoferritins.
The Journal of biological chemistry    July 25, 1975   Volume 250, Issue 14 5446-5449 
Ishitani K, Listowsky I.Horse spleen ferritin was fractionated into its constituent isoferritins by isoelectric focusing. Separated isoferritins were stable and showed no tendency to redistribute when re-examined by analytical gel focusing. All of the isoferritins were immunologically indistinguishable when tested with antibodies raised against unfractionated horse spleen ferritin. The separated isoferritins also had similar conformations as determined by circular dichroism. Iron distribution studies, however, revealed a wide disparity among the isoferritins. The most acidic components had the lowest iron content but...
ATPase activity and filament formation of partially purified myosin from leucocytes.
Journal of biochemistry    July 1, 1975   Volume 78, Issue 1 93-103 
Takeuchi K, Shibata N, Senda N.Myosin was isolated from leucocytes in horse arterial blood by the same procedures used for the isolation of myosin from skeletal muscle. The Ca2+-, EDTA-, and Mg2+-ATPase [EC 3.6.1.3] activities of the protein was 0.148, 0.147, and 0.001 mumoles/min/mg, respectively, in 0.5 M KCl at pH 7.0 and 25 degrees. The Ca2+-ATPase activity decreased with decrease in the ionic strength. No difference was found between leucocyte myosin and skeletal myosin in the pH profiles of Ca2+- and EDTA-ATPases. The rate and amount of the initial burst of Pi liberation of leucocyte myosin were 0.002 mumoles/min/mg a...
Inhibition of horse muscle acylphosphatase by pyridoxal 5′-phosphate.
Biochimica et biophysica acta    June 24, 1975   Volume 391, Issue 2 486-493 doi: 10.1016/0005-2744(75)90272-7
Ramponi G, Manao G, Camici G, White GF.It has been shown that horse muscle acylphosphatase is inhibited by pyridoxal 5'-phosphate and that the inhibition is pH dependent, reversible and competitive with respect to substrate binding. Spectral analysis on the EI complex demonstrates the presence of a Schiff base. Reduction of the pyridoxal 5'-phosphate-inhibited enzyme with sodium borohydride, followed by amino acid analysis, produces a diminution of the free lysine peak and the appearance of a new peak corresponding to epsilon-pyridoxyllysine. The results suggest that there is at least one NH2-lysyl residue of horse muscle acylphosp...
Structure of horse-spleen apoferritin at 6 angstom resolution.
Nature    June 19, 1975   Volume 255, Issue 5510 653-654 doi: 10.1038/255653a0
Hoare RJ, Harrison PM, Hoy TG.No abstract available
Constituents of ceramide monohexoside isolated from equine kidney.
The Japanese journal of experimental medicine    June 1, 1975   Volume 45, Issue 3 231-234 
Kojima H, Tamai Y.No abstract available
Comparison of the myoglobin of the zebra (Equus burchelli) with that of the horse (Equus caballus).
Biochimica et biophysica acta    May 30, 1975   Volume 393, Issue 1 201-204 doi: 10.1016/0005-2795(75)90232-9
Darbre PD, Romero-Herrera AE, Lehmann H.The tryptic and peptic peptides from the myoglobin of the zebra (Equus burchelli) have been compared with those obtained from the myoglobin of the horse (Equus caballus). No differences in the myoglobin were found between these two species.
Carboxymethyl horse-liver alcohol dehydrogenase. Ligand-binding and kinetic properties of the cysteine-46-modified enzyme.
Archives of biochemistry and biophysics    May 1, 1975   Volume 168, Issue 1 145-162 doi: 10.1016/0003-9861(75)90237-4
Reynolds CH, McKinley-McKee JS.No abstract available
Identification of O-cetylated N-acylneuraminic acids by mass spectrometry.
Carbohydrate research    May 1, 1975   Volume 41 7-17 doi: 10.1016/s0008-6215(00)87002-0
Kamerling JP, Vliegenthart JF.A number of O-acetylated N-acylneuraminic acids, isolated from submandibular glands of cow and horse and from horse erythrocytes, have been characterized by mass spectrometry. On the basis of the typical fragmentation patterns of the pertrimethylsilyl derivatives of the methyl esters of the compounds, they were identified as 4-O-acetyl-, 9-O-acetyl-, 4,9-di-O-acetyl-, and 7,9-di-O-acetyl N-acetylneuraminic acid, and 4-O-acetyl-and 9-O-acetyl-N-glycolylneuraminic acid.
Manganese-substituted hemoglobin and myoglobin.
Annals of the New York Academy of Sciences    April 15, 1975   Volume 244 174-186 doi: 10.1111/j.1749-6632.1975.tb41530.x
Hoffman BM, Gibson QH, Bull C, Crepeau RH, Edelstein SJ, Fisher RG, McDonald MJ.No abstract available
The use of prostaglandins in reproduction.
The Canadian veterinary journal = La revue veterinaire canadienne    April 1, 1975   Volume 16, Issue 4 97-101 
Wenkoff MS.No abstract available
Species variability in the modification of erythrocyte surface proteins by enzymatic probes.
Biochimica et biophysica acta    March 13, 1975   Volume 382, Issue 2 181-192 doi: 10.1016/0005-2736(75)90176-5
Carraway KL, Colton DG, Shin BC, Triplett RB.Bovine and equine erythrocytes have been studied by three different surface modification techniques to investigate the accessibility of the surface components to the external medium. Lactoperoxidase labeling of equine erythrocytes results in a significant labeling of only one membrane component, a 100 000-mol.wt polypeptide corresponding to the membrane-spanning Component III of human erythrocytes. The major sialoglycoprotein of the equine erythrocyte is not labeled. This is in contradistinction to the situation for human and bovine cells, where both components are labeled. The equine membrane...
Hemoglobin genetics in bovines and equines.
Indian journal of biochemistry & biophysics    March 1, 1975   Volume 12, Issue 1 51-57 
Lalthantluanga R, Gulati JM, Barnabas J.No abstract available
Mercuri-nitrophenol as a reporter group for the conformational change of hemoglobin.
Journal of biochemistry    March 1, 1975   Volume 77, Issue 3 595-604 doi: 10.1093/oxfordjournals.jbchem.a130761
Yagisawa S.One mole of horse hemoglobin tetramer reacts with 2 moles of 2-chloromercuri-4-nitrophenol (MNP) at beta 93 cysteine. The difference spectra between NMP-bound hemoglobin and hemoglobin, measured with the aid of ascorbic acid and ascorate oxidase [EC 1.10.3.3] as deoxygenation reagents, indicate that the pK of the phenolic hydroxyl group of MNP increases by 0.6 to 0.8 pH unit on deoxygenation of the hemoglobin. The Hill constant of the modified hemoglobin changes with pH. It decreases from about 2.4 at pH 6.8 to about 1.0 at pH 9.0 This effect of the reagent is interpreted as inherent to the re...