Analyze Diet
The Biochemical journal1968; 109(1); 19-24; doi: 10.1042/bj1090019

Amino acid sequences around the cystine residues in horse growth hormone.

Abstract: 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.
Publication Date: 1968-08-01 PubMed ID: 4876100PubMed Central: PMC1186747DOI: 10.1042/bj1090019Google Scholar: Lookup
The Equine Research Bank provides access to a large database of publicly available scientific literature. Inclusion in the Research Bank does not imply endorsement of study methods or findings by Mad Barn.
  • Journal Article

Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

This research study deals with the identification of the specific amino acid sequences that surround the cystine residues in horse growth hormone. The researchers isolated the cystine-containing peptides of horse growth hormone and ascertained their amino acid sequences, finding two different peptides with unique sequences.

Isolation and Identification of Amino Acid Sequences

  • The researchers first isolated the cystine-containing peptides of horse growth hormone. Cystine is a sulfur-containing amino acid, which is known to play a critical role in protein structure.
  • After isolating these peptides, the researchers determined their amino acid sequences. Amino acid sequencing is a chemical method used to determine the sequence of amino acids in a protein, peptide, or a single amino acid.
  • They discovered that four unique half-cystine residues occur in two peptides, one containing 11 and the other, at the C-terminus (the end part of an amino acid chain) of the protein, containing 15 amino acids. This suggests that these sequences are particularly important in the structure and function of horse growth hormone.

Comparison with Other Species’ Growth Hormones

  • The identified amino acid sequences were then compared with already published data on growth hormones from other species.
  • This comparative step is key in making inter-species comparisons, understanding evolutionary relationships, and discerning the general principles of growth hormone structure and function across different species.
  • The results of this comparison, while not provided in the abstract, would have shed light on commonalities and differences across species, and possibly hint at any relation between specific sequence patterns around cystine residues and hormone function.

Implications and Significance

  • This research gives insight into the specific sequences surrounding cystine residues in horse growth hormones, which will provide a greater understanding of how these hormones function and possibly lead to breakthroughs in veterinary medicine.
  • By comparing these sequences with growth hormones from other species, researchers can gain a better understanding of the evolution of these hormones, potentially aiding in the development of therapeutic strategies for hormone-related health issues across different species.

Cite This Article

APA
Oliver L, Hartree AS. (1968). Amino acid sequences around the cystine residues in horse growth hormone. Biochem J, 109(1), 19-24. https://doi.org/10.1042/bj1090019

Publication

ISSN: 0264-6021
NlmUniqueID: 2984726R
Country: England
Language: English
Volume: 109
Issue: 1
Pages: 19-24

Researcher Affiliations

Oliver, L
    Hartree, A S

      MeSH Terms

      • Amino Acid Sequence
      • Amino Acids / analysis
      • Animals
      • Cattle
      • Chromatography, Paper
      • Chymotrypsin
      • Cystine
      • Electrophoresis
      • Endopeptidases
      • Growth Hormone / analysis
      • Horses
      • Humans
      • Imines
      • Pepsin A
      • Peptides / analysis
      • Species Specificity
      • Trypsin

      References

      This article includes 16 references
      1. RYLE AP, SANGER F, SMITH LF, KITAI R. The disulphide bonds of insulin.. Biochem J 1955 Aug;60(4):541-56.
        pubmed: 13249947doi: 10.1042/bj0600541google scholar: lookup
      2. Saxena BB, Henneman PH. Preparation and properties of growth hormone from equine pituitary glands.. Endocrinology 1966 Mar;78(3):561-7.
        pubmed: 4286623doi: 10.1210/endo-78-3-561google scholar: lookup
      3. Santomé JA, Wolfenstein C, Paladini AC. C-terminal sequence of amino acids in bovine growth hormone.. Biochem Biophys Res Commun 1965 Aug 16;20(4):482-5.
        pubmed: 5860164doi: 10.1016/0006-291x(65)90604-2google scholar: lookup
      4. WALEY SG, WATSON J. The action of trypsin on polylysine.. Biochem J 1953 Sep;55(2):328-37.
        pubmed: 13093686doi: 10.1042/bj0550328google scholar: lookup
      5. Santomé JA, Wolfenstein CE, Paladini AC. Partial sequence of the first nine amino acids from the C-terminal end in bovine growth hormone.. Biochim Biophys Acta 1965 Nov 15;111(1):342-3.
        pubmed: 5867334doi: 10.1016/0304-4165(65)90506-4google scholar: lookup
      6. MILLS JB, WILHELMI AE. SULFITOLYSIS OF BOVINE GROWTH HORMONE.. Endocrinology 1965 Mar;76:522-5.
        pubmed: 14263291doi: 10.1210/endo-76-3-522google scholar: lookup
      7. RAFTERY MA, COLE RD. Tryptic cleavage at cysteinyl peptide bonds.. Biochem Biophys Res Commun 1963 Mar 25;10:467-72.
        pubmed: 13990433doi: 10.1016/0006-291x(63)90381-4google scholar: lookup
      8. Brown JR, Hartley BS. Location of disulphide bridges by diagonal paper electrophoresis. The disulphide bridges of bovine chymotrypsinogen A.. Biochem J 1966 Oct;101(1):214-28.
        pubmed: 5971783doi: 10.1042/bj1010214google scholar: lookup
      9. Mills JB. C-terminal sequence of pig growth hormone.. Nature 1967 Feb 11;213(5076):631-2.
        pubmed: 6032264doi: 10.1038/213631a0google scholar: lookup
      10. GRAY WR, HARTLEY BS. THE STRUCTURE OF A CHYMOTRYPTIC PEPTIDE FROM PSEUDOMONAS CYTOCHROME C-551.. Biochem J 1963 Nov;89:379-80.
        pubmed: 14084623doi: 10.1042/bj0890379google scholar: lookup
      11. Offord RE. Electrophoretic mobilities of peptides on paper and their use in the determination of amide groups.. Nature 1966 Aug 6;211(5049):591-3.
        pubmed: 5968723doi: 10.1038/211591a0google scholar: lookup
      12. HIRS CH. The oxidation of ribonuclease with performic acid.. J Biol Chem 1956 Apr;219(2):611-21.
        pubmed: 13319283
      13. Hartree AS, Kovacić N, Thomas M. Growth-promoting and luteotrophic activities of human growth hormone.. J Endocrinol 1965 Oct;33(2):249-58.
        pubmed: 4284763doi: 10.1677/joe.0.0330249google scholar: lookup
      14. Wallis M. A C-terminal sequence from ox growth hormone.. Biochim Biophys Acta 1966 Feb 28;115(2):423-8.
        pubmed: 5943443doi: 10.1016/0304-4165(66)90440-5google scholar: lookup
      15. Dixon JS, Li CH. Retention of the biological potency of human pituitary growth hormone after reduction and carbamidomethylation.. Science 1966 Nov 11;154(3750):785-6.
        pubmed: 5919448doi: 10.1126/science.154.3750.785google scholar: lookup
      16. AMBLER RP. THE AMINO ACID SEQUENCE OF PSEUDOMONAS CYTOCHROME C-551.. Biochem J 1963 Nov;89(2):349-78.
        pubmed: 14084622doi: 10.1042/bj0890349google scholar: lookup

      Citations

      This article has been cited 0 times.