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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.
Analysis of a horse family with a crossing-over between the ELA complex and the A blood group system.
Animal genetics    January 1, 1988   Volume 19, Issue 1 1-9 doi: 10.1111/j.1365-2052.1988.tb00782.x
Guerin G, Varewyck H, Bertaud M, Chasset P.A horse family in which a recombination occurred in the chromosome region coding for the serological specificities of the ELA complex and those of the A blood group system of a mare was further analysed by mixed lymphocyte reaction (MLR) and Southern blot hybridization. This family consisted of a stallion, a mare and five full sibs. The stallion and the mare were heterozygous for internationally recognized ELA specificities while only the mare was heterozygous for the A blood group system. MLR between all members of the family confirmed that the stallion possessed two different ELA haplotypes ...
Heparan sulfate proteoglycan from human and equine glomeruli and tubules.
The International journal of biochemistry    January 1, 1988   Volume 20, Issue 12 1391-1400 doi: 10.1016/s0020-711x(98)90007-6
van den Heuvel LP, Veerkamp JH, Monnens LA, Schröder CH.1. Proteoglycans were isolated from human and equine glomeruli or tubules by guanidine extraction and anion exchange chromatography. 2. These proteoglycan preparations contained about equal amounts of heparan sulfate and chondroitin sulfates. 3. During the preparation of glomerular or tubular basement membranes the main part of proteoglycans (greater than 50%) was extracted in the salt extract. Chondroitin sulfate proteoglycan was mainly found in the water and salt extracts of glomeruli and tubules, heparan sulfate proteoglycan in the deoxycholate extracts and the basement membranes. 4. The gl...
Restriction fragment length polymorphisms of horse class II MHC genes observed using various human alpha- and beta-chain cDNA probes.
Animal genetics    January 1, 1988   Volume 19, Issue 4 395-408 doi: 10.1111/j.1365-2052.1988.tb00831.x
Hänni K, Hesford F, Lazary S, Gerber H.Genomic DNA isolated from 20 horses was digested with up to six restriction endonucleases and subjected to southern blot hybridization analysis using various human class II alpha- and beta-chain cDNA probes. A high degree of restriction fragment length polymorphism (RFLP) was found for the DQ alpha, DP beta, DQ beta and DR beta probes, about 20 polymorphic bands being detected for each. DR alpha showed 2-4 polymorphic bands, whereas no evidence for DP alpha-like genes was found. A number of correlations of RFLPs with individual alloantisera were apparent.
At least two loci encode polymorphic class I MHC antigens in the horse.
Animal genetics    January 1, 1988   Volume 19, Issue 4 379-390 doi: 10.1111/j.1365-2052.1988.tb00829.x
Donaldson WL, Crump AL, Zhang CH, Kornbluth J, Kamoun M, Davis W, Antczak DF.Six monoclonal antibodies and ten alloantisera were used to precipitate cell surface molecules of approximately 44 kDa (class I MHC antigens) from radiolabelled equine peripheral blood lymphocytes. All ten antisera were raised against antigens of a single donor horse (horse 0834, ELA-A2,-A2). Four methods of producing antisera were compared: one or two pregnancies, skin allografting, and skin grafting followed by pregnancy. Immunization by pregnancy appeared to produce antibodies against class I products only, while skin grafting raised antibodies to class II antigens as well. Nine of the anti...
Structural aspects of the plasminogen of various species.
Enzyme    January 1, 1988   Volume 40, Issue 2-3 63-69 doi: 10.1159/000469147
Schaller J, Rickli EE.The N-terminal amino acid sequence of equine, ovine, canine, goat and rabbit plasminogen were determined and compared with those already known of the human, bovine, porcine and feline molecule. Furthermore, the kringle 4 domains of equine, ovine, canine and goat plasminogen, prepared by limited cleavage with elastase, were sequenced and compared with the known species of human, bovine, porcine and chicken plasminogen. Homology with the human kringle 4 ranges between 73% (chicken) and 90% (bovine). Comparison of sequences, fragmentation patterns with elastase and adsorption on lysine-Bio-Gel su...
Iodide-induced inhibition of adenylate cyclase activity in horse and dog thyroid.
European journal of biochemistry    December 30, 1987   Volume 170, Issue 1-2 435-442 doi: 10.1111/j.1432-1033.1987.tb13718.x
Cochaux P, Van Sande J, Swillens S, Dumont JE.The characteristics of the iodide-induced inhibition of cyclic AMP accumulation in dog thyroid slices have been previously described [Van Sande, J., Cochaux, P. and Dumont, J. E. (1985) Mol. Cell. Endocrinol. 40, 181-192]. In the present study we investigated the characteristics of the iodide-induced inhibition of adenylate cyclase activity in dog and horse thyroid. The inhibition of cyclic AMP accumulation by iodide in stimulated horse thyroid slices was similar to that observed in dog thyroid slices. The inhibition was observed in slices stimulated by thyroid-stimulating hormone, cholera tox...
Reconstituted and native iron-cores of bacterioferritin and ferritin.
Journal of molecular biology    December 5, 1987   Volume 198, Issue 3 405-416 doi: 10.1016/0022-2836(87)90290-7
Mann S, Williams JM, Treffry A, Harrison PM.The structural and magnetic properties of the iron-cores of reconstituted horse spleen ferritin and Azotobacter vinelandii bacterioferritin have been investigated by high-resolution transmission electron microscopy, electron diffraction and Mossbauer spectroscopy. The structural properties of native horse spleen ferritin, native Az. vinelandii, and native and reconstituted Pseudomonas aeruginosa bacterioferritins have also been determined. Reconstitution in the absence of inorganic phosphate at pH 7.0 showed sigmoidal behaviour in each protein but was approximately 30% faster in initial rate f...
Characterization of a homogeneous paraprotein from a horse with spontaneous multiple myeloma syndrome.
Veterinary immunology and immunopathology    December 1, 1987   Volume 17, Issue 1-4 69-77 doi: 10.1016/0165-2427(87)90128-0
Seide RK, Jacobs RM, Dobblestein TN, Kehoe JM.A novel myeloma paraprotein has been isolated from a horse with a lymphoid tumor. The protein was a euglobulin and consequently was readily isolated from serum in pure form and high yield by simple dilution in distilled water. The purified intact protein had a molecular weight of 150,000 and was composed of heavy and light chains, both of which had blocked amino-termini and were thus not susceptible to amino-terminal sequence analysis. The amino acid compositions of these respective chains corresponded to those of comparable chains from immunoglobulins of other species. Peptide maps of parapro...
The major protamine from stallion sperm. Isolation and amino-acid sequence.
Biological chemistry Hoppe-Seyler    December 1, 1987   Volume 368, Issue 12 1619-1626 doi: 10.1515/bchm3.1987.368.2.1619
Ammer H, Henschen A.The major stallion protamine was isolated from sperm cell nuclei by extraction with 6M guanidine/5% mercaptoethanol, alkylation with 4-vinylpyridine and subsequent reversed-phase high-performance liquid chromatography. The primary structure of stallion protamine was determined by N-terminal sequencing of the intact protein and of the fragments obtained from thermolysin cleavage of the S-pyridylethylated and from endoproteinase Lys-C cleavage of the S-aminoethylated protein. Stallion protamine consists of 49 amino-acid residues and shows 49% identity with all other sequenced mammalian type 1 pr...
Nucleotide (cDNA) sequence encoding the horse gonadotrophin alpha-subunit.
The Journal of endocrinology    November 1, 1987   Volume 115, Issue 2 341-346 doi: 10.1677/joe.0.1150341
Stewart F, Thomson JA, Leigh SE, Warwick JM.Several cDNA clones corresponding to mRNA for the alpha-subunit of the horse (Equus caballus) pituitary and placental (chorionic) gonadotrophic hormones have been isolated and sequenced. Polyadenylated mRNA was purified from horse pituitary glands (the source of FSH and LH) and horse placental tissues (the source of chorionic gonadotrophin; CG). The mRNA preparations were characterized by in-vitro translation and Northern hybridization techniques using human and ovine gonadotrophin cDNA clones as probes. Complementary DNA libraries were created from the pituitary and placental mRNAs and a huma...
[Isolation and purification of proteolytic enzymes on organo-silica sorbents with immobilized gramicidin S].
Ukrainskii biokhimicheskii zhurnal (1978)    November 1, 1987   Volume 59, Issue 6 28-33 
Ignatchenko AP, Bogomaz VI, TugaÄ­ VA, ChuÄ­ko AA.Biospecific sorbents for affinity chromatography of proteolytic enzymes have been synthesized by attaching cyclopeptide antibiotic gramicidin S to organo-silica supports. It is shown possible to attach gramicidin S to the organo-silica supports using glutaric aldehyde, p-benzoquinone, soluble and insoluble carbodiimides. The sorbents prepared by these methods were successfully applied for the purification of the crude pepsin from horse gastric juice and proteolytic complex produced by Acremonium chrysogenum.
Binding of horse heart cytochrome c to yeast porphyrin cytochrome c peroxidase: a fluorescence quenching study on the ionic strength dependence of the interaction.
Archives of biochemistry and biophysics    November 1, 1987   Volume 258, Issue 2 621-629 doi: 10.1016/0003-9861(87)90385-7
Vitello LB, Erman JE.The binding of horse heart cytochrome c to yeast cytochrome c peroxidase in which the heme group was replaced by protoporphyrin IX was determined by a fluorescence quenching technique. The association between ferricytochrome c and cytochrome c peroxidase was investigated at pH 6.0 in cacodylate/KNO3 buffers. Ionic strength was varied between 3.5 mM and 1.0 M. No binding occurs at 1.0 M ionic strength although there was a substantial decrease in fluorescence intensity due to the inner filter effect. After correcting for the inner filter effect, significant quenching of porphyrin cytochrome c pe...
Structural polypeptides of equine arteritis virus.
Nihon juigaku zasshi. The Japanese journal of veterinary science    October 1, 1987   Volume 49, Issue 5 923-925 doi: 10.1292/jvms1939.49.923
Iwashita O, Harasawa R.No abstract available
Can the product of the theta gene be a real globin?
Nature    October 1, 1987   Volume 329, Issue 6138 465-466 doi: 10.1038/329465a0
Clegg JB.A new member (theta 1, or psi alpha) of the alpha-globin gene family has recently been identified in a number of species. In higher primates the theta 1 gene has all the structural features apparently necessary for expression, and it appears to have long been under strong selective constraints which suggests that it could still be, or recently have been, a functional gene. No corresponding 'globin' has yet been identified, however. In some other species, galago and rabbit for example, the theta 1 and psi alpha genes have accumulated enough inactivating mutations for them to be considered genui...
Gene conversions in the horse alpha-globin gene complex.
Molecular biology and evolution    September 1, 1987   Volume 4, Issue 5 492-503 doi: 10.1093/oxfordjournals.molbev.a040456
Clegg JB.The sequences of the linked alpha 2- and alpha 1-globin genes of the equine BI and BII haplotypes are greater than 99% identical within a 1.2-kb region extending from approximately 75 bp upstream of the putative cap site to a point approximately 150 bp 3' to the poly A addition signal. Differences between the alpha 2 and alpha 1 genes that are common to both haplotypes indicate that a major gene conversion occurred approximately 12 Myr ago and that this has been followed by shorter, more localized, conversions. Interhaplotype (allelic) comparisons at the alpha loci suggest that the BI and BII ...
Ethoxyformylation of histidine residues in equine growth hormone.
International journal of peptide and protein research    September 1, 1987   Volume 30, Issue 3 365-370 doi: 10.1111/j.1399-3011.1987.tb03343.x
Fukushima JG, Cascone O, Santomé JA, Biscoglio de Jimenez Bonino MJ.Reactivity of histidine residues in equine growth hormone to ethoxyformic anhydride was studied. The existence of two kinetically different sets was demonstrated: one of them including only the slow reacting histidine 169 (k = 0.164 min-1) and the other containing fast reacting histidines 19 and 21 (k = 0.892 min-1). A correlation between the decrease in the capacity to compete with 125I-labeled hormone for rat liver binding sites and the degree of ethoxyformylation of the fast group was found. Circular dichroism studies indicated no significant conformational changes in the protein with all t...
Site-directed chemical modification of horse cytochrome c results in changes in antigenicity due to local and long-range conformational perturbations.
The Journal of biological chemistry    August 25, 1987   Volume 262, Issue 24 11591-11597 
Cooper HM, Jemmerson R, Hunt DF, Griffin PR, Yates JR, Shabanowitz J, Zhu NZ, Paterson Y.Comparative binding studies with peptide fragments of the whole antigen, or with evolutionarily related intact proteins with varying degrees of sequence homology, have been used extensively to map antigenic sites on proteins to the resolution of single amino acid residues. These methods are limited, however, since high affinity antibodies will often not react with peptides and evolutionarily related proteins are available for only a few antigens. In this study we use site-directed chemical modification of horse cytochrome c to identify residues involved in the binding sites of four monoclonal ...
Identification of the ligand-exchange process in the alkaline transition of horse heart cytochrome c.
The Biochemical journal    August 15, 1987   Volume 246, Issue 1 43-54 doi: 10.1042/bj2460043
Gadsby PM, Peterson J, Foote N, Greenwood C, Thomson AJ.Magnetic-circular-dichroism (m.c.d.) spectra over the wavelength range 300-2000 nm at room temperature and at 4.2K of horse heart cytochrome c are reported at a series of pH values between 7.8 and 11.0, encompassing the alkaline transition. The effect of glassing agents on the e.p.r. spectrum at various pH values is also reported. Comparison of these results with spectra obtained for the n-butylamine adduct of soybean leghaemoglobin support the hypothesis that lysine is the sixth ligand in the alkaline form of horse heart cytochrome c. The m.c.d. and e.p.r. spectra of horse heart cytochrome c ...
Structural and functional studies on ferritins.
Biochemical Society transactions    August 1, 1987   Volume 15, Issue 4 744-748 doi: 10.1042/bst0150744
Harrison PM, Ford GC, Rice DW, Smith JM, Treffry A, White JL.No abstract available
The role of aromatic side chain residues in micelle binding by pancreatic colipase. Fluorescence studies of the porcine and equine proteins.
The Biochemical journal    August 1, 1987   Volume 245, Issue 3 821-829 doi: 10.1042/bj2450821
McIntyre JC, Hundley P, Behnke WD.Fluorescence techniques have been employed to study the interaction of porcine and equine colipase with pure taurodeoxycholate and mixed micelles. Nitrotyrosine-55 of porcine colipase is obtained by modification with tetranitromethane (low excess, in the presence of taurodeoxycholate) of the protein followed by gel filtration and ion-exchange chromatography. Verification of the residue modified was obtained by h.p.l.c. peptide purification and sequence analysis. Reduction and quantitative reaction with dansyl chloride yields a fluorescent derivative that is twice as active in conjunction with ...
The binding domain on horse cytochrome c and Rhodobacter sphaeroides cytochrome c2 for the Rhodobacter sphaeroides cytochrome bc1 complex.
Biochemistry    July 14, 1987   Volume 26, Issue 14 4501-4504 doi: 10.1021/bi00388a049
Hall J, Zha XH, Yu L, Yu CA, Millett F.The interaction of the Rhodobacter sphaeroides cytochrome bc1 complex with Rb. sphaeroides cytochrome c2 and horse cytochrome c was studied by using specific lysine modification and ionic strength dependence methods. The rate of the reactions with both cytochrome c and cytochrome c2 decreased rapidly with increasing ionic strength above 0.2 M NaCl. The ionic strength dependence suggested that electrostatic interactions were equally important to the reactions of the two cytochromes, even though they have opposite net charges at pH 7.0. In order to define the interaction domain on horse cytochro...
The amino acid sequence of an amyloid fibril protein AA isolated from the horse.
Scandinavian journal of immunology    July 1, 1987   Volume 26, Issue 1 79-84 doi: 10.1111/j.1365-3083.1987.tb02237.x
Sletten K, Husebekk A, Husby G.The amino acid sequence of the amyloid fibril protein AA from horse was established from characterization of cyanogen bromide fragments, tryptic peptides, and a peptide derived from a digest with Staphylococcus aureus V8 proteinase. The protein was found to consist of 80 amino acid residues. Sequence homologies with protein AA from other species were very striking, and revealed an insertion of two amino acid residues between positions 72 and 73. In position 44, two amino acid residues were found which provide further evidence for a polymorphism in the amyloid fibril protein AA.
Proton hyperfine resonance assignments using the nuclear Overhauser effect for ferric forms of horse and tuna cytochrome c.
Biophysical journal    July 1, 1987   Volume 52, Issue 1 101-107 doi: 10.1016/S0006-3495(87)83193-4
Satterlee JD, Moench S.Proton hyperfine resonance assignments for cytochromes c from several species are currently being successfully pursued by several laboratories. These efforts focus mostly on the ferrous forms. In contrast to that work, we have pursued assignments of the proton hyperfine shifted resonances for horse and tuna ferricytochromes c. Our results indicate that assignments are nearly identical in those two proteins. Using the pre-steady state nuclear Overhauser effect, several additional assignments have been made for the tuna protein, whereas for the horse protein, the following protons have been assi...
Structural studies on equine glycoprotein hormones. Amino acid sequence of equine chorionic gonadotropin beta-subunit.
The Journal of biological chemistry    June 25, 1987   Volume 262, Issue 18 8603-8609 
Sugino H, Bousfield GR, Moore WT, Ward DN.The complete amino acid sequence of the beta-subunit of equine chorionic gonadotropin (eCG beta) has been established by both automated Edman and manual 5-dimethylaminonaphthalene-1-sulfonyl-Edman degradations. Specific fragments were produced by cleavage with Staphylococcus aureus V8 protease, trypsin, or dilute HCl. For the sequence analyses of the heavily glycosylated COOH-terminal portion, a chemical deglycosylation procedure with trifluoromethanesulfonic acid was employed. The peptide chain of eCG beta consists of 149 amino acid residues. Five or more oligosaccharide chains are attached t...
Structural studies on equine glycoprotein hormones. Amino acid sequence of equine lutropin beta-subunit.
The Journal of biological chemistry    June 25, 1987   Volume 262, Issue 18 8610-8620 
Bousfield GR, Liu WK, Sugino H, Ward DN.The amino acid sequence was determined for equine lutropin beta (eLH beta). Large fragments were derived from reduced, carboxymethylated eLH beta by digestion with Staphylococcus aureus V8 protease, by cyanogen bromide cleavage, and by cleavage of acid-labile Asp-Pro bonds. The fragments were purified by gel filtration and high performance liquid chromatography (HPLC). The fragments were sequenced by automated Edman degradation to establish the primary structure of eLH beta. Some peptides were further digested with chymotrypsin and the resulting peptides purified by HPLC. In addition to sequen...
Calmodulin-mediated adenylate cyclase from mammalian sperm.
The Journal of biological chemistry    June 25, 1987   Volume 262, Issue 18 8672-8676 
Gross MK, Toscano DG, Toscano WA.Calmodulin (CaM), the calcium binding protein that modulates the activity of a number of key regulatory enzymes, is present at high levels in sperm. To determine whether CaM regulates adenylate cyclase in mammalian sperm, the actions of EGTA and selected CaM antagonists on a solubilized adenylate cyclase from mature equine sperm were examined. The activity of equine sperm adenylate cyclase was inhibited by EGTA in a concentration-dependent manner with a half-maximal inhibitory concentration (IC50) of 2 mM. Equine sperm adenylate cyclase was also inhibited in a concentration-dependent manner by...
Isolation and characterization of two protamines St1 and St2 from stallion spermatozoa, and amino-acid sequence of the major protamine St1.
Biochimica et biophysica acta    June 17, 1987   Volume 913, Issue 2 145-149 doi: 10.1016/0167-4838(87)90323-2
Bélaïche D, Loir M, Kruggle W, Sautière P.Two protamines, St1 and St2, were isolated from stallion sperm nuclei, where they represent about 75 and 25%, respectively, of the total basic protein complement. The primary structure of protamine St1 (49 residues; Mr approximately equal to 6600) has been determined. The structure of this protamine is compared to the amino-acid sequence of other mammalian protamines already known.
[Equine herpesvirus 1 (EHV-1) infection in the horse: neurologic symptoms in a standard bred mare with acute fatal course. Molecular characterization of the brain isolates and pathologic correlates].
Berliner und Munchener tierarztliche Wochenschrift    May 1, 1987   Volume 100, Issue 5 147-152 
Ludwig H, Rudolph R, Chowdhury SI, van den Bossche G, Wintzer HJ, Krauser K.No abstract available
Regulation of equine herpesvirus type 1 gene expression: characterization of immediate early, early, and late transcription.
Virology    May 1, 1987   Volume 158, Issue 1 79-87 doi: 10.1016/0042-6822(87)90240-6
Gray WL, Baumann RP, Robertson AT, Caughman GB, O'Callaghan DJ, Staczek J.The regulation of equine herpesvirus type 1 (EHV-1) transcription was examined in infected rabbit kidney cells using metabolic inhibitors. In order to map EHV-1 immediate early, early, and late transcripts, viral RNA was 32P-labeled in vivo and hybridized to EHV-1 DNA restriction fragments immobilized on nitrocellulose filters. Immediate early viral RNA was mapped to one region of the viral genome within the inverted repeat DNA sequences (map units 0.78-0.83 and 0.95-1.0). Northern blot hybridization analysis using a 32P-labeled cloned DNA probe from this region identified a single immediate e...
Aromatization of 19-norandrogens by equine testicular microsomes.
The Journal of biological chemistry    April 25, 1987   Volume 262, Issue 12 5717-5722 
Gaillard JL, Silberzahn P.In the stallion testis, aromatase activity was localized in the microsomal fraction. Androgen aromatization occurred through the loss of 1 beta,2 beta hydrogen atoms and appeared to involve free sulfhydryl groups. A single enzyme system seemed to aromatize androgen and norandrogen at the same rate while having a much lower affinity for norandrogens.