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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.
[Middle peptide sequence obtained by cleaving horse myoglobin with cyanogen bromide].
Bulletin de la Societe de chimie biologique    July 25, 1969   Volume 51, Issue 3 439-455 
Han K, Boulanger Y, Dautrevaux M, Biserte G.No abstract available
Optical rotatory dispersion and circular dichroism of horse myoglobin and its derivatives.
Journal of biochemistry    May 1, 1969   Volume 65, Issue 5 759-766 doi: 10.1093/oxfordjournals.jbchem.a129075
Samejima T, Kita M.No abstract available
[Corecipitation: methods for analysing monovalent antibody fragments. I. Equine antidiphtheria system: hyperimmune sera].
Annales de l'Institut Pasteur    May 1, 1969   Volume 116, Issue 5 657-685 
Iscaki S, Raynaud M.No abstract available
Measurement of ligand-induced conformational changes in hemoglobin by circular dichroism.
Proceedings of the National Academy of Sciences of the United States of America    May 1, 1969   Volume 63, Issue 1 205-212 doi: 10.1073/pnas.63.1.205
Simon SR, Cantor CR.The UV circular-dichroism spectra of human and horse hemoglobins have been determined at various degrees of partial saturation with oxygen. Spectra of the two native hemoglobins were compared with spectra of the corresponding proteins modified with a reagent known to eliminate the conformational rearrangement normally associated with cooperativity. Such comparison indicates that one region, around 260 mmu, is sensitive chiefly to the state of the hemes; changes in another region, around 285 mmu, may be correlated with the conformational transformation linked to cooperative interactions. All ci...
Horse muscle acyl phosphatase: purification and some properties.
Archives of biochemistry and biophysics    March 1, 1969   Volume 130, Issue 1 362-369 doi: 10.1016/0003-9861(69)90045-9
Ramponi G, Guerritore A, Treves C, Nassi P, Baccari V.No abstract available
Binding of long chain alkyl sulphates to equine ferric myoglobin.
European journal of biochemistry    March 1, 1969   Volume 8, Issue 2 263-272 doi: 10.1111/j.1432-1033.1969.tb00523.x
van den Oord AH, Wesdorp JJ.When ferric myoglobin reacts with alkyl sulphates, its absorption spectrum changes into one characteristic of a haemichrome or parahaematin. The reaction equilibrium was studied over a range of protein concentrations using dodecyl sulphate and other alkyl sulphates with different chain lengths. The results obtained from spectrophotometric measurements and equilibrium dialysis experiments are not in agreement with those of other authors who, from an analysis of spectral changes only, supported the hypothesis of an all-or-none type of reaction whereby 18 detergent anions were bound to one molecu...
Studies on tissue culture of equine ovarian cell types: pathways of steroidogenesis.
The Journal of endocrinology    March 1, 1969   Volume 43, Issue 3 403-414 doi: 10.1677/joe.0.0430403
Channing CP.No abstract available
Studies on tissue culture of equine ovarian cell types: steroidogenesis.
The Journal of endocrinology    March 1, 1969   Volume 43, Issue 3 391-402 doi: 10.1677/joe.0.0430391
Channing CP, Grieves SA.No abstract available
Equine antihapten antibody. The molecular weights of the subunits of equine immunoglobulins.
Biochemistry    March 1, 1969   Volume 8, Issue 3 1247-1258 doi: 10.1021/bi00831a060
Montgomery PC, Dorrington KJ, Rockey JH.Three independent methods have been used to determine the molecular weights of the heavyand light-polypeptide chain subunits of equine yGab-, yGc-, and yT-immunoglobulins. Extensively reduced and alkylated proteins were filtered through standard columns of Sephadex G-100 or G-200 in 8 M urea405 M propionic acid. Subunit molecular weights were obtained from the linear elution volume, V,, us. logarithm molecular weight relationship defined for each column with rabbit yG-globulin heavy and light chains and horse heart cytochrome c. Molecular weights also were determined by equilibrium se...
The nucleic acid content of skeletal muscle and liver in mammals of different body size.
Comparative biochemistry and physiology    February 1, 1969   Volume 28, Issue 2 897-905 doi: 10.1016/0010-406x(69)92123-9
Munro HN, Gray JA.No abstract available
Granular localization of corticotropin-releasing activity in horse hypophysial stalk homogenate.
Endocrinologia japonica    February 1, 1969   Volume 16, Issue 1 171-177 doi: 10.1507/endocrj1954.16.171
Ishii S, Iwata T, Kobayashi H.No abstract available
[Structure of peptides isolated from chymotrypsin hydrolysates of horse myoglobin].
Bulletin de la Societe de chimie biologique    January 30, 1969   Volume 50, Issue 10 1651-1669 
Boulanger Y, Dautrevaux M, Han K, Biserte G.No abstract available
Equine immunoglobulins: a comparison of molecular properties.
Acta biochimica Polonica    January 1, 1969   Volume 16, Issue 3 279-296 
Buchowicz I, Goch H, Zakrzewski K.No abstract available
Cleavage of horse immunoglobulin by cyanogen bromide.
Immunochemistry    November 1, 1968   Volume 5, Issue 6 513-524 doi: 10.1016/0019-2791(68)90088-8
Ernst ML, Arnon R, Sela M.No abstract available
Succinylcholine analogs as substrates and inhibitors of pseudocholinesterase.
Journal of medicinal chemistry    November 1, 1968   Volume 11, Issue 6 1126-1128 doi: 10.1021/jm00312a005
Beckett AH, Vaughan CL, Mitchard M.No abstract available
The binding of plutonium to serum proteins in vitro.
Radiation research    October 1, 1968   Volume 36, Issue 1 22-30 
Turner GA, Taylor DM.The interactions between tetravalent plutonium and horse serum proteins were studied in vitro by electrophoresis on cellulose acetate and by gel filtration. The results show that in horse serum, as in other mammalian sera, the plutonium is associated principally with the transferrin component of the beta1-globulins. The formation of the plutonium-transferrin complex requires the presence of HCO3-, and plutonium is displaced from the complex by excess iron, thus indicating that similar binding sites may be involved in the complexing of iron and plutonium. The plutonium complex is considered to ...
Action of horse urinary kallikrein on synthetic derivatives of bradykinin.
Biochemical pharmacology    October 1, 1968   Volume 17, Issue 10 2232-2234 doi: 10.1016/0006-2952(68)90200-1
Babel I, Stella RC, Prado ES.Previous experiments indicated that horse urinary kallikrein (UK) hydrolyzes salminei- e and polyarginine, a but not polylysine. This paper reports the action of UK on bradykinyl-serine, methionyllysyl-bradykinin and lysyllysyl-bradykinin.
Comparison of protein structure in the crystal and in solution. V. Solubility of horse methemoglobin and azide binding.
Journal of molecular biology    August 14, 1968   Volume 35, Issue 3 477-481 doi: 10.1016/s0022-2836(68)80007-5
Rupley JA, Gates V.No abstract available
Some properties of soluble proteins from chromaffin granules of different species.
Biochemical pharmacology    August 1, 1968   Volume 17, Issue 8 1553-1556 doi: 10.1016/0006-2952(68)90214-1
Strieder N, Ziegler E, Winkler H, Smith AD.No abstract available
Amino acid sequences around the cystine residues in horse growth hormone.
The Biochemical journal    August 1, 1968   Volume 109, Issue 1 19-24 doi: 10.1042/bj1090019
Oliver L, Hartree AS.The cystine-containing peptides of horse growth hormone were isolated and their amino acid sequences determined. Four unique half-cystine residues occur in two peptides, one containing 11 and the other, at the C-terminus of the protein, 15 amino acids. These sequences are compared with published data on growth hormones from other species.
The synthesis of some analogues of butyrylcholine and their hydrolysis by a purified horse serum cholinesterase.
Biochemical pharmacology    August 1, 1968   Volume 17, Issue 8 1591-1594 doi: 10.1016/0006-2952(68)90219-0
Beckett AH, Vaughan CL, Mitchard M.No abstract available
Equine antihapten antibody. VI. Subunits of polyalanylated gamma-G(T)-immunoglobulin.
Biochemistry    July 1, 1968   Volume 7, Issue 7 2462-2468 doi: 10.1021/bi00847a003
Genco RJ, Karush F, Tenenhouse HS.No abstract available
A mutant form of lactate dehydrogenase in the horse.
Annals of the New York Academy of Sciences    June 14, 1968   Volume 151, Issue 1 672-677 doi: 10.1111/j.1749-6632.1968.tb11927.x
Rauch N.No abstract available
Horse spleen apoferritin: N-terminal and C-terminal residues.
Archives of biochemistry and biophysics    June 1, 1968   Volume 125, Issue 3 975-980 doi: 10.1016/0003-9861(68)90536-5
Mainwaring WI, Hofmann T.No abstract available
The correlation of serum levels of two transaminases with tissue levels in six vertebrate species.
Comparative biochemistry and physiology    June 1, 1968   Volume 25, Issue 3 1081-1089 doi: 10.1016/0010-406x(68)90593-8
Zimmerman HJ, Dujovne CA, Levy R.No abstract available
Structure and function of haemoglobin. IV. A three-dimensional Fourier synthesis of horse deoxyhaemoglobin at 5.5 A resolution.
Journal of molecular biology    April 14, 1968   Volume 33, Issue 1 283-297 doi: 10.1016/0022-2836(68)90294-5
Bolton W, Cox JM, Perutz MF.No abstract available
The mechanism of the inhibitory influence of phosphorolysis on hydrolysis of glycogen in the muscles of domestic animals.
Archivum immunologiae et therapiae experimentalis    January 1, 1968   Volume 16, Issue 1 116-136 
Iwanowski H.No abstract available
[Amino acid content of horse and sheep gamma-G-globulins and their peptide chains].
Biokhimiia (Moscow, Russia)    January 1, 1968   Volume 33, Issue 1 25-28 
Zhumaschev Zh, Seitov ZS.No abstract available
Comparative analysis of the IgG heavy chain carbohydrate peptide.
Journal of molecular biology    December 28, 1967   Volume 30, Issue 3 555-558 doi: 10.1016/0022-2836(67)90369-5
Howell JW, Hood L, Sanders BG.No abstract available
The reaction of carbon monoxide with horse hemoglobin in solution, in erythrocytes, and in crystals.
The Journal of biological chemistry    December 25, 1967   Volume 242, Issue 23 5762-5770 
Parkhurst LJ, Gibson QH.No abstract available