Analyze Diet

Topic:Amino Acid Sequence

Amino acid sequences in horses refer to the specific order of amino acids in a protein, which is crucial for determining the protein's structure and function. These sequences are encoded by the horse's genetic material and are essential for various biological processes, including muscle development, enzyme activity, and immune response. Understanding amino acid sequences in horses can provide insights into genetic diseases, performance traits, and overall health. This topic explores the latest research on equine amino acid sequences, focusing on their role in protein synthesis, genetic variation, and implications for breeding and veterinary medicine. The page compiles peer-reviewed studies and scholarly articles that investigate the significance of amino acid sequences in equine biology.
Sequence of a cDNA encoding horse growth hormone.
Gene    June 10, 1994   Volume 143, Issue 2 299-300 doi: 10.1016/0378-1119(94)90115-5
Ascacio-Martínez JA, Barrera-Saldaña HA.A cDNA encoding horse growth hormone (ecGH) was isolated and sequenced. The coding sequence resembles a typical mammalian GH pre-protein and contains a 3' untranslated region of 101 nucleotides carrying two contiguous polyadenylation signals.
Structure of the equine infectious anemia virus Tat protein.
Science (New York, N.Y.)    June 10, 1994   Volume 264, Issue 5165 1584-1587 doi: 10.1126/science.7515512
Willbold D, Rosin-Arbesfeld R, Sticht H, Frank R, Rösch P.Trans-activator (Tat) proteins regulate the transcription of lentiviral DNA in the host cell genome. These RNA binding proteins participate in the life cycle of all known lentiviruses, such as the human immunodeficiency viruses (HIV) or the equine infectious anemia virus (EIAV). The consensus RNA binding motifs [the trans-activation responsive element (TAR)] of HIV-1 as well as EIAV Tat proteins are well characterized. The structure of the 75-amino acid EIAV Tat protein in solution was determined by two- and three-dimensional nuclear magnetic resonance methods and molecular dynamics calculatio...
Identification of the horse epidermal growth factor (EGF) coding sequence and its use in monitoring EGF gene expression in the endometrium of the pregnant mare.
Journal of molecular endocrinology    June 1, 1994   Volume 12, Issue 3 341-350 doi: 10.1677/jme.0.0120341
Stewart F, Power CA, Lennard SN, Allen WR, Amet L, Edwards RM.The PCR technique and highly degenerate oligonucleotide primers were used to amplify a 282 bp fragment of the horse (Equus caballus) epidermal growth factor (EGF) cDNA. The clone corresponded to 94 amino acids of the EGF precursor molecule. The deduced amino acid sequence of the 53 residue EGF mitogenic peptide within the precursor sequence showed 60-70% identity with five other published EGF sequences. The PCR cDNA fragment hybridized to a 4.9 kb transcript in horse kidney and endometrial RNA which was of a similar size to the mature EGF transcript found in other mammalian species. The horse ...
Serological and genomic characterization of equine rotavirus VP4 proteins identifies three different P serotypes.
Virology    June 1, 1994   Volume 201, Issue 2 364-372 doi: 10.1006/viro.1994.1302
Isa P, Snodgrass DR.A series of viral reassortants was prepared between equine rotaviruses H1 (G5), H2 (G3), and L338 (G13) and human rotavirus ST3 (G4). All contained the VP4 cognate gene segment 4 from the equine parental virus and the VP7 cognate gene segment 9 from ST3. Using these viruses and antisera prepared to them, it was shown that each of the three equine viruses possessed a serologically distinct VP4 or P serotype with a > or = 16-fold difference in reciprocal cross-neutralization titers. H1 VP4 was closely related to that of porcine virus OSU, i.e., P7. L338 gene 4 was sequenced, and the sequence and...
Structural and functional characterization of elastases from horse neutrophils.
The Biochemical journal    June 1, 1994   Volume 300 ( Pt 2), Issue Pt 2 401-406 doi: 10.1042/bj3000401
Dubin A, Potempa J, Travis J.In order better to understand the pathophysiology of the equine form of emphysema, two elastinolytic enzymes from horse neutrophils, referred to as proteinases 2A and 2B, have been extensively characterized and compared with the human neutrophil proteinases, proteinase-3 and elastase. Specificity studies using both the oxidized insulin B-chain and synthetic peptides revealed that cleavage of peptide bonds with P1 alanine or valine residues was preferred. Further characterization of the two horse elastases by N-terminal sequence and reactive-site analyses indicated that proteinases 2A and 2B ha...
Comparison of M and N gene sequences distinguishes variation amongst equine arteritis virus isolates.
The Journal of general virology    June 1, 1994   Volume 75 ( Pt 6) 1491-1497 doi: 10.1099/0022-1317-75-6-1491
Chirnside ED, Wearing CM, Binns MM, Mumford JA.cDNA copies of the M and N genes of equine arteritis virus (EAV) isolates were synthesized by reverse transcription followed by polymerase chain reaction amplification. The cDNA was subjected to a cycle sequencing strategy using Taq polymerase, and the nucleotide and derived amino acid sequences of 10 virus isolates were compared. The M and N genes of all isolates had the same initiation and termination sites as the prototype Bucyrus strain and the encoded proteins were conserved between viruses. Comparison of nucleotide sequence homologies and phylogenetic tree analysis implied the existence ...
Isolation, primary structures and metal binding properties of neuronal growth inhibitory factor (GIF) from bovine and equine brain.
FEBS letters    May 30, 1994   Volume 345, Issue 2-3 193-197 doi: 10.1016/0014-5793(94)00452-8
Pountney DL, Fundel SM, Faller P, Birchler NE, Hunziker P, Vasák M.Human neuronal growth inhibitory factor (GIF) impairs the survival of cultured neurons and is deficient in the brains of Alzheimer's disease victims. We have isolated and sequenced analogous proteins from bovine and equine brain. By comparing their primary structures with those of human, mouse and rat GIFs, a consensus GIF sequence was obtained. Although this exhibits ca. 65% similarity with primary structures of mammalian metallothioneins (MTs), some significant differences are expected in the content of helix and turn secondary structures. In contrast to MTs, which usually bind 7 Zn(II) ions...
Cloning and sequencing of the equine testicular follitropin receptor.
Biochemical and biophysical research communications    May 30, 1994   Volume 201, Issue 1 201-207 doi: 10.1006/bbrc.1994.1689
Robert P, Amsellem S, Christophe S, Benifla JL, Bellet D, Koman A, Bidart JM.To investigate the possibility that specific structural determinants within the equine follitropin receptor (eFSHR) are critical to the enhanced specificity of this receptor compared to other FSHRs, we used the RACE-PCR technique to clone the eFSHR from equine testis. Sequence analysis revealed that the eFSHR is highly homologous to other mammal FSHRs, but it presents 10 unique amino acid residue replacements in the extracellular domain. Furthermore, a potential N-glycosylation site was detected at a position not encountered in other receptors. Northern blot analysis identified three transcrip...
A versatile synthetic peptide-based ELISA for identifying antibody epitopes.
Journal of immunological methods    May 2, 1994   Volume 171, Issue 1 37-44 doi: 10.1016/0022-1759(94)90226-7
Ball JM, Henry NL, Montelaro RC, Newman MJ.A simple, versatile and very inexpensive procedure for cross-linking synthetic peptides to the polystyrene surfaces of micro-well assay plates for use in ELISA was developed. The method is based on the use of poly-L-lysine (PLL) as the anchor protein for synthetic peptides which were then easily and covalently linked to the PLL using glutaraldehyde. The synthetic peptides used for the study were based on the amino acid sequence of the equine infectious anemia virus (EIAV) envelope sequence and evaluated as antigens in an ELISA designed to detect antibodies in serum of EIAV-infected horses and ...
Species specificity and interspecies relatedness in VP4 genotypes demonstrated by VP4 sequence analysis of equine, feline, and canine rotavirus strains.
Virology    May 1, 1994   Volume 200, Issue 2 390-400 doi: 10.1006/viro.1994.1203
Taniguchi K, Urasawa T, Urasawa S.We determined the nucleotide and deduced amino acid sequences of the VP4 genes of five equine, two feline, and two canine rotavirus strains. A high degree of homology (> 97.0%) was found among the VP4 amino acid sequences of the equine strains H2, FI-14, and FI23. Equine strain L338 has a distinct VP4 amino acid sequence from those of the other equine strains (78.1% or less homology), and the L338 VP4 exhibited more than 17.0% divergence at the amino acid level from those of rotavirus strains published so far. The VP4 amino acid sequence of equine strain H1, which showed low homology with t...
Identification of phosphoseryl residues in protamines from mature mammalian spermatozoa.
Biology of reproduction    May 1, 1994   Volume 50, Issue 5 981-986 doi: 10.1095/biolreprod50.5.981
Pirhonen A, Linnala-Kankkunen A, Mäenpää PH.Protamines isolated from ejaculated human, stallion, bull, boar, and ram spermatozoa were subjected to phosphoserine conversion reaction and protein sequencing. Phosphoserines were detected as S-ethylcysteines. Endogenously phosphorylated protamines have previously been found only in ejaculated human sperm. In this study, we demonstrate that ejaculated sperm from other species also contain protamines phosphorylated at serine residues. In P1-protamines, the endogenously phosphorylated serines were located at the N-terminal region in all species studied, whereas in major forms of human and stall...
Rapid refolding of native epitopes on the surface of cytochrome c.
Biochemistry    April 5, 1994   Volume 33, Issue 13 3967-3973 doi: 10.1021/bi00179a024
Allen MJ, Jemmerson R, Nall BT.Refolding of surface epitopes on horse cytochrome c has been measured by monoclonal antibody binding. Two antibodies were used to probe re-formation of native-like surface structure: one antibody (2B5) binds to native cytochrome c near a type II turn (residue 44) while the other (5F8) binds to a different epitope on the opposite face of the protein near the amino terminus of an alpha-helical segment (residue 60). The results show that within the first approximately 100 ms of refolding all of the unfolded protein collapses to native-like folding intermediates that contain both antibody binding ...
Molecular cloning and sequencing of equine interleukin 4.
Veterinary immunology and immunopathology    April 1, 1994   Volume 40, Issue 4 379-384 doi: 10.1016/0165-2427(94)90047-7
Vandergrifft EV, Swiderski CE, Horohov DW.We have cloned equine interleukin 4 (IL-4) cDNA using the polymerase chain reaction (PCR) and primers based on the human IL-4 sequence. The cDNA was amplified from mitogen-stimulated equine peripheral blood mononuclear cells (PBMC). The cloned PCR product shares extensive homology ith IL-4 sequences from other species.
Posttranscriptional effector domains in the Rev proteins of feline immunodeficiency virus and equine infectious anemia virus.
Journal of virology    March 1, 1994   Volume 68, Issue 3 1998-2001 doi: 10.1128/JVI.68.3.1998-2001.1994
Mancuso VA, Hope TJ, Zhu L, Derse D, Phillips T, Parslow TG.By systematically dissecting the Rev proteins of feline immunodeficiency virus (FIV) and equine infectious anemia virus (EIAV), we have identified within each a short peptide that is functionally interchangeable with the effector domains found in Rev-like proteins from other retroviruses. The active sequences from FIV and EIAV differ in several respects from other known effectors and may represent a distinct class of effector domain.
Structure determination of the disialylated poly-(N-acetyllactosamine)-containing O-linked carbohydrate chains of equine chorionic gonadotropin.
Glycoconjugate journal    February 1, 1994   Volume 11, Issue 1 35-41 doi: 10.1007/BF00732430
Hokke CH, Roosenboom MJ, Thomas-Oates JE, Kamerling JP, Vliegenthart JF.The disialylated poly-(N-acetyllactosamine)-containing O-linked oligosaccharide alditols, released by alkaline borohydride treatment of the enzymically N-deglycosylated beta-subunit of equine chorionic gonadotropin, were purified by fast protein liquid chromatography (FPLC) on Mono Q and analysed by fast ion bombardment mass spectrometry (FAB-MS) and 1H-NMR spectroscopy. The identified oligosaccharide alditols have the following structure: [Formula: see text]
Expression cloning of an equine T-lymphocyte glycoprotein CD2 cDNA. Structure-based analysis of conserved sequence elements.
European journal of biochemistry    February 1, 1994   Volume 219, Issue 3 969-976 doi: 10.1111/j.1432-1033.1994.tb18579.x
Tavernor AS, Kydd JH, Bodian DL, Jones EY, Stuart DI, Davis SJ, Butcher GW.An equine CD2 cDNA has been isolated by monoclonal antibody screening of a T-lymphocyte cDNA library. The cDNA contained an open reading frame of 1041 bp encoding a translated product of 347 amino acids. Northern blotting analysis revealed a single mRNA species expressed in spleen, thymus and activated peripheral lymphocytes. The predicted amino acid sequence has 50-65% identity with the human, rat and mouse CD2 sequences with greatest similarity shared with the human homologue. Evolutionarily conserved structural and functional domains in CD2 were identified by comparing the sequences of the ...
Polymorphism in the coding sequence of the horse transferrin gene.
Genome    February 1, 1994   Volume 37, Issue 1 157-165 doi: 10.1139/g94-020
Carpenter MA, Broad TE.Transferrin, the iron transport protein of the blood, is highly polymorphic in many species, including the horse. A number of sequence polymorphisms that distinguish several of the variants of horse transferrin are reported here. Previous studies indicated that exons 12 and 15 were likely to be polymorphic. Sequencing regions of exons 12 and 15 from D and R variants revealed 10 nucleotide substitutions that encoded six amino acid replacements. The F1, F2, H2, and * variants were identical to D, and the O variant was almost identical to R, in the regions studied. The data indicated that the hor...
Molecular cloning and characterization of horse DQB cDNA.
Immunogenetics    January 1, 1994   Volume 40, Issue 6 458 doi: 10.1007/BF00177831
Szalai G, Antczak DF, Gerber H, Lazary S.No abstract available
Molecular cloning and characterization of horse DQA cDNA.
Immunogenetics    January 1, 1994   Volume 40, Issue 6 457 doi: 10.1007/BF00177830
Szalai G, Antczak DF, Gerber H, Lazary S.No abstract available
Nucleotide sequence of the equine interferon gamma cDNA.
DNA sequence : the journal of DNA sequencing and mapping    January 1, 1994   Volume 4, Issue 6 405-407 doi: 10.3109/10425179409010190
Curran JA, Argyle DJ, Cox P, Onions DE, Nicolson L.Interferon gamma, a cytokine produced by T-lymphocytes and natural killer cells, plays a central role in the modulation of the immune response, and its antiviral and antitumourigenic properties have made it a potential candidate for use in immunoprophylactic and therapeutic regimes. We have cloned the equine IFN gamma cDNA to facilitate production of this cytokine for clinical evaluation in the horse. The predicted equine IFN gamma amino acid sequence is 67% identical to that of the human equivalent and 78% to the bovine equivalent.
The equine placenta and equine chorionic gonadotrophin–an overview.
Experimental and clinical endocrinology    January 1, 1994   Volume 102, Issue 3 235-243 doi: 10.1055/s-0029-1211287
Hoppen HO.Chorionic gonadotrophins seem to be unique for primate and equid species. Unlike primates, the equine conceptus does not implant in the maternal uterine endometrium until around day 37 of pregnancy. At this time specialized cells of the trophoblast, organized in the embryonic girdle, invade the endometrium and become established in the endometrial stroma, forming the so-called endometrial cups. This migration of girdle cells is accompanied by their morphological transformation into large decidual-like cells and by the appearance of a gonadotrophic hormone in the mare's blood. There is convinci...
Cloning and sequencing of horse interferon-gamma cDNA.
Immunogenetics    January 1, 1994   Volume 39, Issue 6 448-449 doi: 10.1007/BF00176167
Grünig G, Himmler A, Antczak DF.No abstract available
Characterization of horse (Equus caballus) T-cell receptor beta chain genes.
Immunogenetics    January 1, 1994   Volume 40, Issue 2 135-144 doi: 10.1007/BF00188177
Schrenzel MD, Watson JL, Ferrick DA.Genes encoding the horse (Equus caballus) T-cell receptor beta chain (TCRB) were cloned and characterized. Of 33 cDNA clones isolated from the mesenteric lymph node, 30 had functionally rearranged gene segments, and three contained germline sequences. Sixteen unique variable segments (TCRBV), 14 joining genes (TCRBJ), and two constant region genes (TCRBC) were identified. Horse TCRBV were grouped into nine families based on similarity to human sequences. TCRBV2 and TCRBV12 were the most commonly represented horse families. Analysis of predicted protein structure revealed the presence of conser...
Immunoreactivity of cytochrome c: antibodies to horse cytochrome c distinguish between sequence-related cytochromes only at the level of the 3-D-structure.
Biochimie    January 1, 1994   Volume 76, Issue 6 465-470 doi: 10.1016/0300-9084(94)90170-8
Leder L, Bosshard HR.It has long been known that antibodies to cytochrome c can distinguish between closely sequence-related cytochromes c. Because the 3-D-structure of the polypeptide chain is virtually identical among eukaryotic cytochromes c, antibody specificity is directed against amino acid substitutions within a common polypeptide folding pattern. The question arises if the specificity is observed at the level of the 3-D-structure (conformational epitopes) and/or at the level of the primary structure (sequential epitopes). Using rabbit sera to horse cytochrome c, we show that discrimination against the host...
Molecular cloning and expression of equine interleukin 2.
Veterinary immunology and immunopathology    December 1, 1993   Volume 39, Issue 4 395-406 doi: 10.1016/0165-2427(93)90070-k
Vandergrifft EV, Horohov DW.We have cloned equine IL-2 cDNA in vitro using the polymerase chain reaction (PCR) and primers based on the human IL-2 sequence. The cloned product appears to contain the entire coding region for equine IL-2 based on homology with other known sequences. When expressed in COS cells, the recombinant product augmented the proliferative response of equine peripheral blood mononuclear cells to concanavalin A, however, it failed to support the continued proliferation of murine CTLL-2 cells. Specific substitutions in those regions associated with p55 and p75 binding appear to account for this species...
Identification of the activation domain of equine infectious anemia virus rev.
Journal of virology    December 1, 1993   Volume 67, Issue 12 7317-7323 doi: 10.1128/JVI.67.12.7317-7323.1993
Fridell RA, Partin KM, Carpenter S, Cullen BR.Several members of the lentivirus family of complex retroviruses have been shown to encode proteins that are functionally equivalent to the Rev posttranscriptional regulatory protein of human immunodeficiency virus type 1 (HIV-1). Furthermore, the domain organization of HIV-1 Rev, featuring a highly basic N-terminal RNA binding domain and a leucin-rich C-terminal effector domain, has also been shown to be highly conserved among Rev proteins derived from not only the primate but also the ovine and caprine lentiviruses. Although it has therefore appeared highly probable that the lentivirus equin...
Partially folded states of equine lysozyme. Structural characterization and significance for protein folding.
Biochemistry    November 9, 1993   Volume 32, Issue 44 11886-11894 doi: 10.1021/bi00095a018
Van Dael H, Haezebrouck P, Morozova L, Arico-Muendel C, Dobson CM.Despite their homologous structure, c-type lysozymes and alpha-lactalbumins have been found to differ profoundly in their unfolding behavior, in that the alpha-lactalbumins readily enter a partially unfolded collapsed state (the "molten globule"), whereas lysozymes unfold cooperatively to a highly unfolded state. The calcium-binding property of lysozyme from equine milk provides an evolutionary link between the two families of proteins. We demonstrate here that equine lysozyme undergoes a two-stage unfolding transition upon heating or in the presence of guanidine hydrochloride that is highly d...
Immunogens of encephalitis viruses.
Veterinary microbiology    November 1, 1993   Volume 37, Issue 3-4 273-284 doi: 10.1016/0378-1135(93)90029-7
Roehrig JT.The equine encephalitis viruses are members of the genus Alphavirus, in the family Togaviridae. Three main virus serogroups represented by western (WEE), eastern (EEE) and Venezuelan equine encephalitis (VEE) viruses cause epizootic and enzootic infection of horses throughout the western hemisphere. All equine encephalitis viruses are transmitted through the bite of an infected mosquito. The first equine encephalitis virus vaccines were produced by virus inactivation. Problems with inadequate inactivation, which may have caused a major epidemic/epizootic of VEE in central America and Texas in ...
Structural and functional characterization of rev-like transcripts of equine infectious anemia virus.
Journal of virology    September 1, 1993   Volume 67, Issue 9 5640-5646 doi: 10.1128/JVI.67.9.5640-5646.1993
Rosin-Arbesfeld R, Rivlin M, Noiman S, Mashiah P, Yaniv A, Miki T, Tronick SR, Gazit A.Three cDNA clones representing structurally distinct transcripts were isolated from a cDNA library prepared from cells infected with equine infectious anemia virus (EIAV) by using a probe representing the S3 open reading frame, which is thought to encode Rev. One species, designated p2/2, contained four exons and was identical to a previously described polycistronic mRNA that encodes Tat. This transcript was predicted to also direct the synthesis of a truncated form of the transmembrane protein and a putative Rev protein whose N-terminal 29 amino acids, derived from env, are linked to S3 seque...
Purification and characterization of a form of P450 from horse liver microsomes.
Journal of biochemistry    September 1, 1993   Volume 114, Issue 3 445-448 doi: 10.1093/oxfordjournals.jbchem.a124195
Komori M, Higami A, Imai Y, Imaoka S, Funae Y.A form of P450 [termed P450(h-1)] was purified from the liver microsomes of a male horse to electrophoretic homogeneity. The specific content of the final P450(h-1) preparation was 14.8 nmol/mg of protein and the recovery was 0.38% of the microsomal P450. The apparent molecular weight of P450(h-1) was 52,000 Da. The absorption spectra of P450(h-1) indicated that P450(h-1) was a low- and high-spin mixed type P450 in the oxidized form. The reconstituted system containing P450(h-1) could catalyze benzphetamine N-demethylation, 7-ethoxycoumarin O-deethylation, and testosterone 16 alpha-hydroxylati...
1 16 17 18 19 20 27