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Topic:Peptides

Peptides are short chains of amino acids that are involved in various biological processes in horses. They function as signaling molecules, influencing physiological activities such as metabolism, immune response, and tissue repair. Peptides can be naturally occurring or synthetically derived, and they may serve as therapeutic agents in veterinary medicine. In equine health, peptides are studied for their potential applications in enhancing performance, supporting recovery, and managing conditions like osteoarthritis. This page compiles peer-reviewed research studies and scholarly articles that explore the structure, function, and potential applications of peptides in the context of equine health and disease management.
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.
Semisynthetic cytochrome c.
Proceedings of the National Academy of Sciences of the United States of America    October 1, 1977   Volume 74, Issue 10 4248-4250 doi: 10.1073/pnas.74.10.4248
Barstow LE, Young RS, Yakali E, Sharp JJ, O'Brien JC, Berman PW, Harbury HA.Horse heart cytochrome c can be split with cyanogen bromide into a heme peptide (residues 1-65) and a nonheme peptide (residues 66-104). In a process involving (i) complex formation between the two fragments and (ii) restoration of the severed peptide linkage, a fully active cytochrome c preparation can be re-formed. Use has been made of this process to couple the heme peptide to peptide 66-104 synthesized by the Merrifield solid-phase procedure. The semisynthetic product formed in this manner is indistinguishable from reconstituted cytochrome c prepared with nonsynthetic peptide 66-104.
Characterization of a retravirus isolated from squirrel monkeys.
Journal of virology    August 1, 1977   Volume 23, Issue 2 384-393 doi: 10.1128/JVI.23.2.384-393.1977
Schochetman G, Fine D, Arthur L, Gilden R, Heberling R.A new retravirus (SMRV) isolated from a squirrel monkey, Saimiri sciureus, has an Mg2+-dependen reverse transcriptase and a buoyant density of 1.17 g/cm3 in sucrose and 1.21 g/cm3 in cesium chloride, similar to the mouse mammary tumor virus and the Mason-Pfizer monkey virus. The polypeptide patter of SMRV as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis was distinct from the reported polypeptide patterns of known retraviruses. Four major polypeptides of molecular weights 40,000, 20,000, 14,000 and 8,000 were resolved in virus propagated in human, mink, and canine cell...
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...
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...
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.
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.
Comparative studies on the gastric glycopeptide in eleven animal species.
Comparative biochemistry and physiology. B, Comparative biochemistry    January 1, 1977   Volume 58, Issue 2 163-165 doi: 10.1016/0305-0491(77)90103-1
Masuda H, Shichijo S, Takeuchi M.1. Glycopeptides in the stomachs of eleven mammalian species, including human, rabbit, horse, cow, pig, goat, sheep, dog, cat, guinea pig and rat were assayed by determining the carbohydrate content of materials which remained after proteolysis. 2. The glycopeptide content was higher in the mucosa than in the muscular layer including serosa, especially in the porcine stomach and the fourth stomachs of the ruminants than in the stomachs of any other animals. 3. The glycopeptide, which was stained with both alcian blue and PAS, was absent or sparingly present in the mucosae of the human, rabbit,...
Active-site labelling of kallikreins by chloromethylketone derivatives.
General pharmacology    August 1, 1976   Volume 7, Issue 2-3 163-166 doi: 10.1016/0306-3623(76)90055-0
Sampaio CA, Prado ES.Ala-Phe-Lys-CH2-Cl is a chloromethylketone derivative which is able to promote the inhibition of several proteolytic enzymes. In this paper the inhibition of horse urinary and plasmatic kallikreins is described and this inhibition is compared to that produced in human plasma kallikrein. This compound was designed based upon the structure of bradykinin. This enzyme substrate system can provide a model for the study of the interactions between bradykinin and its receptor. The inhibition of the enzymes was achieved both for its esterase and kinin-releasing activities.
Detection of immunologically active zones in equine growth hormone.
European journal of immunology    June 1, 1976   Volume 6, Issue 6 409-417 doi: 10.1002/eji.1830060607
Poskus E, Zakin MM, Fernámdez HN, Paladini AC.Peptide fragments, obtained from equine growth hormone by cyanogen bromide cleavage and further chemical treatment, were isolated and identified. Their immunological reactivities were tested by hemagglutination and complement fixation methods using rabbit antisera against native hormone. Antigenic determinants were detected in the fragments comprising amino acid sequences 5-72 and 73-123, this last one being predominant. Fragment 124-178 had very low reactivity. Nitration of peptide 73-123 did not modify its immunological properties,but oxidation diminished them. Comparison of the antigenicity...
Cell-free synthesis of equine herpesvirus type 3 nucleocapsid polypeptides.
Virology    February 1, 1976   Volume 69, Issue 2 751-762 doi: 10.1016/0042-6822(76)90503-1
Allen GP, Bryans JT.No abstract available
N-acetylserine in horse muscle acylphosphatase.
International journal of peptide and protein research    January 1, 1976   Volume 8, Issue 3 269-273 
Cappugi G, Chellini PC, Nassi P, Ramponi G.A ninhydrin-negative peptide fraction obtained from tryptic digest of carboxymethyl acylphosphatase was isolated by chromatography on a column of PA 28 Beckman resin and analysed for the amino acid composition. Degradation with carboxypeptidase B and A indicated that the sequence of this peptide was: X-Thr-Ala-Arg. The amino-terminal residue was identified as N-acetylserine by high voltage electrophoresis. It is therefore suggested that the sequence of the NH2-terminal portion of CM-acylphosphatase is N-acetyl-Ser-Thr-Ala-Arg. Digestion with carboxypeptidase A and B indicated also that the COO...
Comparison of the myoglobin of the zebra (Equus burchelli) with that of the horse (Equus caballus).
Biochimica et biophysica acta    May 30, 1975   Volume 393, Issue 1 201-204 doi: 10.1016/0005-2795(75)90232-9
Darbre PD, Romero-Herrera AE, Lehmann H.The tryptic and peptic peptides from the myoglobin of the zebra (Equus burchelli) have been compared with those obtained from the myoglobin of the horse (Equus caballus). No differences in the myoglobin were found between these two species.
Conformational studies of equilibrium structures in fragments of horse heart cytochrome c.
European journal of biochemistry    January 2, 1975   Volume 50, Issue 2 367-374 doi: 10.1111/j.1432-1033.1975.tb09812.x
Toniolo C, Fontana A, Scoffone E.Ultraviolet absorption and circular dichroism studies have been carried out on horse heart apo-cytochrome c and heme-free peptide fragments obtained by cyanogen bromide cleavage of the native protein. It was noted that the various peptides assume predominantly an unordered conformation in water solution. Increasing ionic strength and addition of 2-chloroethanol increase the right-handed helical content. Guanidinium hydrochloride favors the coil state. It was also demonstrated that two non-interacting helical regions of different stability are present in the apo-protein in 2-chloroethanol.
Reconstitution of horse heart cytochrome c: reformation of the peptide bond linking residues 65 and 66.
Biochemical and biophysical research communications    December 23, 1974   Volume 61, Issue 4 1400-1406 doi: 10.1016/s0006-291x(74)80439-0
Corradin G, Harbury HA.No abstract available
Alkaline isomerization of ferricytochrome c: identification of the lysine ligand.
Proceedings of the National Academy of Sciences of the United States of America    July 1, 1974   Volume 71, Issue 7 2892-2894 doi: 10.1073/pnas.71.7.2892
Wilgus H, Stellwagen E.Changes in the visible absorbance spectra of complexes of horse heart cytochrome c hemopeptide 1-65, peptide 66-104, and their guanidinated counterparts are compared with those characteristic of native and fully guanidinated ferricytochrome c over the pH range 7 to 11. Upon raising the pH, the methionine ligand in the guanidinated hemopeptide 1-65.peptide 66-104 complex is replaced by a strong field ligand. By contrast, the methionine ligand in the hemopeptide 1-65.guanidinated peptide 66-104 is replaced by a weak field ligand. These results demonstrate that lysine 13 does not ligate with the ...
On the limited peptic digestion of horse heart cytochrome C. isolation of C-terminal peptide sequences.
International journal of peptide and protein research    January 1, 1974   Volume 6, Issue 3 145-148 doi: 10.1111/j.1399-3011.1974.tb02371.x
Fontana A, Vita C, Toniolo C.No abstract available
The organ-specificity of ferritin in human and horse liver and spleen.
The Biochemical journal    January 1, 1973   Volume 131, Issue 1 51-59 doi: 10.1042/bj1310051
Crichton RR, Millar JA, Cumming RL, Bryce CF.1. Ferritin was isolated from human and horse spleen and liver, and apoferritin prepared therefrom. 2. The electrophoretic mobilities of the four apoferritins were determined on polyacrylamide gels and on cellulose acetate strips, and all found to be equal. 3. Homologous ferritins share reactions of identity in immunodiffusion experiments, whereas heterologous ferritins show only partial identity. 4. The subunit molecular weight of each of the apoferritins was determined by polyacrylamide-gel electrophoresis in sodium dodecyl sulphate and by chromatography on agarose columns in 6m-guanidine-HC...
Primary structures of the proinsulin connecting peptides of the rat and the horse.
The Journal of biological chemistry    December 25, 1972   Volume 247, Issue 24 7936-7940 
Tager HS, Steiner DF.No abstract available
Synthetic peptides related to horse heart cytochrome c. VII. Synthesis and inhibitory properties of the 70-80 undecapeptide.
Journal of the American Chemical Society    March 8, 1972   Volume 94, Issue 5 1720-1723 doi: 10.1021/ja00760a050
Wolman Y, Schejter A, Sokolovsky M.No abstract available
Gene expression in an interspecific hybrid: analysis of hemoglobins in donkey, horse, and mule by peptide mapping.
Biochemical genetics    February 1, 1970   Volume 4, Issue 1 73-85 doi: 10.1007/BF00484019
Isaacs WA.No abstract available
[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
[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
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.
[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
Release of human and horse fibrinopeptides.
Acta chemica Scandinavica    January 1, 1967   Volume 21, Issue 7 1879-1886 doi: 10.3891/acta.chem.scand.21-1879
Teger-Nilsson AC.No abstract available
Comparison of the structure of the immunoglobulins from horse serum.
The Biochemical journal    July 1, 1966   Volume 100, Issue 1 63-68 doi: 10.1042/bj1000063
Weir RC, Porter RR.A study of the chemical structure of the horse immunoglobulins IgG and IgA(T) has shown that the amino acid contents of the peptide chains are very similar. These globulins differ most markedly in the products of papain digestion. IgG gives 3.5s products, whereas IgA(T) gives a 5s fraction and smaller components. This difference appears to be associated with the presence of an additional easily reducible disulphide bond in the Fd fragment of the heavy chain. There is two to three times as much carbohydrate in IgA(T) as in IgG. In both, this is in the heavy chain and in IgA(T) more than half is...
[Study of some oligopeptides isolated from chymotrypsin hydrolysates of horse myoglobin globin].
Bulletin de la Societe de chimie biologique    January 1, 1966   Volume 48, Issue 5 733-735 
Boulanger Y, Dautrevaux M, Han KK, Biserte G.No abstract available
[Study of the “median” peptide freed from horse myoglobin by cyanogen bromide].
Bulletin de la Societe de chimie biologique    January 1, 1966   Volume 48, Issue 8 995-997 
Han K, Dautrevaux M, Boulanger Y, Biserte G.No abstract available