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.
Purification of horse renal kallikrein and chemical relations with horse urinary kallikrein.
Advances in experimental medicine and biology    January 1, 1979   Volume 120A 325-333 doi: 10.1007/978-1-4757-0926-1_31
Porcelli G, Marini-Bettolo GB, Croxatto HR, Di Jorio M.Kallikrein was purified from horse kidney by several steps of chromatographic procedure and by affinity chromatography on Sepharose-Concanavaline. Horse urinary kallikrein was previously purified by DE-32 hydroxylapatite and by Sephadex G-100 gel filtration. On the purified final sample of renal and urinary kallikrein the aminoacid composition and the gel electrophoretic molecular weight were determined. The ratio in micronMoles between each aminoacid residue of both hydrolyzed renal and urinary kallikrein of horse is about 1,00 +/- 0,30. Except for Pro, 1/2 Cys and basic aminoacid residues a ...
The binding of FSH, LH and PMSG to equine gonadal tissues.
Journal of reproduction and fertility. Supplement    January 1, 1979   Issue 27 431-440 
Stewart F, Allen WR.Gonadotrophin-receptor binding studies involving the use of 125I-labelled highly purified FSH and LH have shown that equine gonadal tissues possess similar numbers of specific FSH and LH receptors per cell as the gonadal tissues of other mammals. However, while rat, cow and pig gonadal tissues were shown to bind as much 125I-labelled PMSG as 125I-labelled LH on a molar basis, the equivalent equine tissues bound only less than or equal to 4% as much of the labelled PMSG as LH. Competitive binding studies involving the use of radioreceptor assay techniques have further demonstrated that the smal...
Hybridization of bovine papilloma virus type 1 and type 2 DNA to DNA from virus-induced hamster tumors and naturally occurring equine tumors.
Intervirology    January 1, 1979   Volume 11, Issue 4 227-233 doi: 10.1159/000149038
Lancaster WD, Theilen GH, Olson C.DNAs from bovine papilloma virus(BPV)-induced hamster tumors and from equine connective tissue tumors of unknown etiology were examined for BPV DNA sequences by molecular hybridization. DNA from two distinct classes of BPV (type 1 and type 2) was labeled in vitro and used as probes. Analysis of DNA-DNA reassociation kinetics indicated that both virus types were capable of tumor induction in the hamster. DNA isolated from 6 of 7 equine tumors accelerated the reassociation of the BPV DNA probes. BPV type 1 or type 2 DNA hybridized extensively to DNA from 3 tumors, while 3 other tumors contained ...
A study of the specificity of Bandeiraea simplicifolia lectin I by competitive-binding assay with blood-group substances and with blood-group A and B active and other oligosaccharides.
Carbohydrate research    November 1, 1978   Volume 67, Issue 1 243-255 doi: 10.1016/s0008-6215(00)83746-5
Kisailus EC, Kabat EA.The specificity of Bandeiraea simplicifolia lectin I (BS I) has been studied by competitive-binding assays (CBA) using tritium-labeled human B and hog A substances. Blood-group B substances isolated from horse gastric mucosae and from human ovarian-cyst fluids were much better inhibitors of binding of tritiated blood-group B substance to insoluble BS I-Sepharose 2B than were human blood-group A substances from saliva and ovarian-cyst fluid. A and B active blood-group substances showed the same range of potency in inhibiting binding of tritium-labeled hog A substance to BS I-Sepharose 2B. CBA w...
Alkaline isomerization of horse and yeast cytochromes C. Spectrophotometric and circular dichroism studies.
International journal of peptide and protein research    November 1, 1978   Volume 12, Issue 5 233-236 
Looze Y, Polastro E, Deconinck M, Leonis J.Spectrophotometric studies of the alkaline isomerization of horse heart and yeast cytochrome c show that the haemoproteins from Saccharomyces cerevisiae differ significantly from the mammalian cytochrome c. Apparent pKa values of 8.41, 8.40 and 8.73 for isol-1-(the methylated and unmethylated forms) and iso-2-cytochrome c respectively, from baker's yeast were determined and compared with the value of 9.40 found for horse heart cytochrome c. The transitions, measured by observing the decrease of the absorbance at 695 nm as the pH increases, have been found to strictly parallel the decrease in a...
Platelet tropomyosin: lack of binding to skeletal muscle troponin and correlation with sequence.
FEBS letters    October 1, 1978   Volume 94, Issue 1 131-135 doi: 10.1016/0014-5793(78)80922-3
Côté GP, Lewis WG, Pato MD, Smillie LB.No abstract available
Fourier transform infrared spectroscopic study of molecular interactions in hemoglobin.
Applied optics    September 15, 1978   Volume 17, Issue 18 2985-2990 doi: 10.1364/AO.17.002985
Alben JO, Bare GH.Infrared absorption spectra of the alpha-104 (G11) cysteine SH group have been observed for aqueous solutions of hemoglobin derivatives from humans, pigs, and horses. The center frequencies ((nu)SH) show ligand sensitive patterns that are similar for the three species, with (nu)SH (HbCO) <(nu)SH (HbO(2) ~ HbCN) < (nu)SH (Hb(+)) <<(nu)SH (deoxyHb) for human and pig hemoglobins. The alpha-104 SH group is most strongly H-bonded (smallest (nu)SH), has the greatest range of (nu)SH (Hb ? HbCO) in human hemoglobin, and is least strongly H-bonded and has the smallest range of (nu)SH (Hb ? HbCO) in hor...
Amino acid sequence of the beta-subunit of the follicle-stimulating hormone from equine pituitary glands.
The Journal of biological chemistry    August 10, 1978   Volume 253, Issue 15 5363-5368 
Fujiki Y, Rathnam P, Saxena BB.A tentative amino acid sequence of the beta-subunit of equine follicle-stimulating hormone (FSH) was derived from the sequences of tryptic, thermolytic as well as peptic, subtilisin, and chymotryptic peptides. Equine FSH-beta is analogous to human FSH-beta except six amino acid substitutions at positions 12, 16, 21, 62, 108, and 114. The amino acid sequence suggests that the hormone-specific beta-subunits of FSH are similar at the interspecies level, whereas the amino acid sequences of the hormone nonspecific alpha-subunits show variations.
Isolation and amino acid sequence of the alpha-subunit of follicle-stimulating hormone from equine pituitary glands.
The Journal of biological chemistry    August 10, 1978   Volume 253, Issue 15 5355-5362 
Rathnam P, Fujiki Y, Landefeld TD, Saxena BB.Six hundred milligrams of follicle-stimulating hormone (FSH), containing 110 NIH-FSH-S1 units/mg, was isolated from 9 kg of equine pituitary glands. The equine FSH was dissociated into alpha- and beta-subunits. A tentative amino acid sequence of the alpha-subunit was determined. The alpha-subunit contained 82 amino acids. The equine FSH-alpha is shorter by 10 to 14 amino acids at the NH2 terminus and has several substitutions at several positions as compared with human FSH-alpha and bovine thyroid-stimulating hormone-alpha. At the intraspecies level, the alpha-subunits of human FSH, human lute...
The presence of two (Na+ + K+)-ATPase inhibitors in equine muscle ATP: vanadate nad a dithioerythritol-dependent inhibitor.
Biochimica et biophysica acta    August 4, 1978   Volume 511, Issue 2 202-212 doi: 10.1016/0005-2736(78)90314-0
Quist EE, Hokin LE.A potent inhibitor of (Na+ + K+)-ATPase activity was purified from Sigma equine muscle ATP by cation- and anion-exchange chromatography. The isolated inhibitor was identified by atomic absorption spectroscopy and proton resonance spectroscopy to be an inorganic vanadate. The isolated vanadate and a solution of V2O5 inhibit sarcolemma (Na+ + K+)-ATPase with an I50 of 1 micrometer in the presence of 1 mM ethyleneglycol-bis-(beta-aminoethylether)-N,N'-tetraacetic acid (EGTA), 145 mM NaCl, 6mM MgCl2, 15 mM KCl and 2 mM synthetic ATP. The potency of the isolated vanadate is increased by free Mg2+. ...
Isolation of a gonadotropin (PMEG) from pregnant mare endometrial cups: comparison with PMSG. Papkoff H, Farmer SW, Cole HH.The gonadotropin (PMEG) in pregnant mare endometrial cups was purified and compared to pregnant mare serum gonadotropin (PMSG). Purification methodology applicable to PMSG was employed. In vivo and in vitro assays for FSH and LH were used to evaluate PMEG preparations. In all cases, lower activities (11-54%) were observed with PMEG compared to PMSG. Antiserum raised in rabbits against PMSG cross-reacts fully with PMEG in agar double diffusion tests. The amino acid composition of PMEG is similar to PMSG, but amino terminal group analyses show PMEG preparations to be more heterogeneous than PMSG...
Detection of proviral DNA in horse cells infected with equine infectious anemia virus.
Journal of virology    June 1, 1978   Volume 26, Issue 3 577-583 doi: 10.1128/JVI.26.3.577-583.1978
Rice NR, Simek S, Ryder OA, Coggins L.Equine infectious anemia virus (EIAV) recently has been shown to possess a high-molecular-weight RNA genome and a virion reverse transcriptase. We completed the demonstration that EIAV is a retrovirus by showing the presence of proviral DNA in equine cells infected in vitro, but not in normal horse DNA. These studies were performed by using a highly representative cDNA probe synthesized by the virion polymerase. It was found that this cDNA reassociated extensively, and with high thermal stability, with either viral RNA or DNA extracted from infected cells, but showed no detectable reassociatio...
[The interaction between phosphate and protein, and the respiration of the llama, the human fetus and the horse (author’s transl)].
Hoppe-Seyler's Zeitschrift fur physiologische Chemie    May 1, 1978   Volume 359, Issue 5 547-558 
Braunitzer G, Schrank B, Stangl A, Bauer C.The sequence analysis of llama (Lama glama, Camelidae) hemoglobin is described. The chains were separated, cleaved by trypsin as previously described, quantitatively characterized and sequenced in the sequenator. The llama hemoglobin differs from the human hemoglobin in that it has 25 different amino acids in the alpha chain and 24 different amino acids in the beta chain. The interaction between protein and phosphate is discussed. The earlier finding that the O2 affinity of the llama hemoglobin is dependent on its content of 2, 3-bisphosphoglycerate is interpreted here as a mutation of the 2, ...
Specific reaction of aloe extract with serum proteins of various animals.
Experientia    April 15, 1978   Volume 34, Issue 4 523-524 doi: 10.1007/BF01935968
Fujita K, Suzuki I, Ochiai J, Shinpo K, Inoue S, Saito H.We found that aloe extract contains a lectin-like substance which reacts with serum proteins of various animals. Furthermore, in human serum 2 proteins, alpha2-macroglobulin and alpha1-antitrypsin, were shown to be reactive with aloe extract.
Ferritin: structure, biosynthesis, and role in iron metabolism.
Physiological reviews    April 1, 1978   Volume 58, Issue 2 317-396 doi: 10.1152/physrev.1978.58.2.317
Munro HN, Linder MC.No abstract available
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...