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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.
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...
[Comparative electrophoretic study of the molecular forms of alkaline phosphatase in the leukocytes of agricultural animals].
Veterinarno-meditsinski nauki    January 1, 1977   Volume 14, Issue 3 100-104 
Goranov Kh.The alkaline phosphatase enzyme, isolated by Morton's method from leukocytes of sheep, goats, and pigs gave after agarose elctrophoresis two isoenzyme fractions moving to the positive pole at the sites of the alpha 1- and alpha 2-globulins of the blood serum. In bovine leukocytes, besides these two fractions there was a third one that moved more slowly in the zone of the beta-globulins. In horses the alkaline phosphatase of leukocytes produced a wide band within the zones of the beta-globulins and the albumins. It was established that the proportion between the individual isoenzyme fractions o...
Identification of the PR prealbumin proteins in horse serum.
Acta veterinaria Scandinavica    January 1, 1977   Volume 18, Issue 4 458-470 doi: 10.1186/BF03548409
Ek N.The Pr protein, which is one of the major equine acidic prealbumins and which consists of a large number of phenotypes, has been studied with regard to its chemical identity. Serum samples of known Pr phenotype which had been treated with varying amounts of bovine trypsin were subjected to starch gel electrophoresis at pH 4.8. When a certain amount of trypsin was used, the Pr protein was markedly affected, whereas the other acidic prealbumins retained their normal electrophoreitic pattern. Extracts from three different regions of the acidic prealbumin field were tested by the casein precipitat...
Proton-dependent dissociation equilibrium of hemoglobin. 1. A 700-nanometer light-scattering study on horse methemoglobin in the pH range 4.8 to 7.2.
Biochemistry    December 28, 1976   Volume 15, Issue 26 5693-5697 doi: 10.1021/bi00671a002
Schroeder E, Wollmer A, Kubicki J, Ohlenbusch HD.The effect of proton concentration upon the subunit dissociation of horse methemoglobin has been investigated at two ionic strengths by light scattering photometry at 700 nm. Differential refractometry revealed a slight but systematic decrease of the specific refractive index increment with decreasing protein concentration for solutions in dialytic equilibrium with the solvent. In the pH range 4.8-7.2 the dissociation can be described by a simple equilibrium between tetramers and dimers. The dissociation constant Kd of the met derivative is found to be very similar to those of the O2- and CO-l...
Copper and the oxidation of hemoglobin: a comparison of horse and human hemoglobins.
Biochemistry    November 30, 1976   Volume 15, Issue 24 5337-5343 doi: 10.1021/bi00669a021
Rifkind JM, Lauer LD, Chiang SC, Li NC.Oxidation studies of hemoglobin by Cu(II) indicate that for horse hemoglobin, up to a Cu(II)/heme molar ratio of 0.5, all of the Cu(II) added is used to rapidly oxidize the heme. On the other hand, most of the Cu(II) added to human hemoglobin at low Cu(II)/heme molar ratios is unable to oxidize the heme. Only at Cu(II)/heme molar ratios greater than 0.5 does the amount of oxidation per added Cu(II) approach that of horse hemoglobin. At the same time, binding studies indicate that human hemoglobin has an additional binding site involving one copper for every two hemes, which has a higher copper...
The purification and kinetic properties of biophosphoglycerate synthase from horse red blood cells.
Archives of biochemistry and biophysics    November 1, 1976   Volume 177, Issue 1 284-292 doi: 10.1016/0003-9861(76)90438-0
Rose AB, Dube S.No abstract available
[Effect of ATP on carbohydrate metabolism].
Veterinariia    November 1, 1976   Issue 11 99-100 
Alekseev MIu.No abstract available
Studies on iron uptake and micelle formation in ferritin and apoferritin.
Molecular and cellular biochemistry    October 30, 1976   Volume 13, Issue 1 55-61 doi: 10.1007/BF01732396
Stefanini S, Chiancone E, Vecchini P, Antonini E.Iron uptake and micelle formation in ferritin and apoferritin have been followed both spectrophotometrically and by means of sedimentation velocity experiments. Information was thus obtained on the molecular weight distribution of the reconstitution product. To achieve incorporation 'native' ferritin (whole ferritin as purified from horse spleen), 'native' apoferritin (apoferritin prepared by fractionation of ferritin preparations) and 'reduced' apoferritin (apoferritin prepared by reduction of ferritin by dithionite or ascorbic acid) have been incubated with ferrous salts in the presence of o...
Amino-acid sequence of equine renal metallothionein-1B.
Proceedings of the National Academy of Sciences of the United States of America    October 1, 1976   Volume 73, Issue 10 3413-3417 doi: 10.1073/pnas.73.10.3413
Kojima Y, Berger C, Vallee BL, Kägi JH.The amino-acid sequence of a metallothionein is reported. Metallothionein is a widely distributed, extremely cysteine-rich, low-molecular-weight protein containing large amounts of cadmium and/or zinc. Metallothionein-1B is one of the two prinicipal variants occurring in equine kidney cortex. The single-chain protein contains 61 amino acids and has the composition Cys20 Ser8Lys7Arg1Ala7Gly5Val3Asp2Asn1-Glu1Gln2Pro2Thr1Met1(Cd + Zn)7. Its amino-terminal residue is N-acetylmethionine. The sequence shows distinct clustering of the twenty cysteinyl residues into seven groups separated by stretches...
[Study of hydrolysis of aminoalcohol ethers, phenol and choline under the action of horse blood serum cholinesterase].
Biokhimiia (Moscow, Russia)    October 1, 1976   Volume 41, Issue 10 1773-1777 
Kundriutskova LA, Kruglikova RI.Hydrolysis of ethers of saturated and unsaturated alcohols and ethers, e.g. phenol and choline, under the action of horse blood serum cholinesterase, was studied. The reactivity towards enzymatic hydrolysis is decreased due to a greater length of the chain in the alcohol residue of the benzoic acid aminoethers; at nCH2 = 4 the compound is a poor substrate. An increase in nydrophobicity of the acyl residue of the ether molecule also leads to a decrease in the Vmax and Km values. In case of cholinesterase substrates, an increase in the molecule hydrophobicity results in an increase of its non-pr...
Characterization of the domestic horse (Equus caballus) karyotype using G- and C-banding techniques.
Experientia    September 15, 1976   Volume 32, Issue 9 1146-1149 doi: 10.1007/BF01927593
Buckland RA, Fletcher JM, Chandley C.No abstract available
Alkali-labile oligosaccharides from glycoproteins of different erythrocyte and milk fat globule membranes.
Biochimica et biophysica acta    September 7, 1976   Volume 443, Issue 3 402-413 doi: 10.1016/0005-2736(76)90460-0
Glöckner WM, Newman RA, Dahr W, Uhlenbruck G.Phenol extraction of horse, sheep, cow, pig and human erythrocyte membranes and human milk fat globule membranes gave glycoprotein fractions, all of which were shown by gas chromatography to contain the reduced disaccharide beta-D-galactosyl (1-3)-N-acetyl-D-galactosaminital after treatment with alkaline borohydride. Cow and pig erythrocyte membrane glycoproteins were found however to contain much lower amounts than the erythrocyte membrane glycoproteins of the other species tested. After gel filtration, a tetrasaccharide was isolated from horse and sheep glycoproteins containing the disacchar...
Equine infectious anemia virus: evidence favoring classification as a retravirus.
Journal of virology    September 1, 1976   Volume 19, Issue 3 1073-1079 doi: 10.1128/JVI.19.3.1073-1079.1976
Charman HP, Bladen S, Gilden RV, Coggins L.Equine infectious anemia virus (EIAV) has a density of 1.154 g/cm3 in sucrose a high-molecular-weight RNA similar in size to Rauscher murine leukemia virus, and an internal virion reverse transcriptase that utilizes the synthetic RNA template poly(rA) but not the synthetic DNA template poly(dA), both with (dT)12 as primer. Although capable of utilizing manganese at low concentrations (approximately 0.1 mM), EIAV reverse transcriptase showed highest activity in the presence of 9 mM magnesium. The major protein of EIAV has a slightly lower molecular weight than the comparable protein of type C v...