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European journal of immunology1976; 6(6); 409-417; doi: 10.1002/eji.1830060607

Detection of immunologically active zones in equine growth hormone.

Abstract: 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 of equine growth hormone fragment 73-123 with that of the homologous ovine growth hormone fragment 86-123 lent support to the hypothesis that at least one antigenic determinant area in the horse hormone fragment is dependent on sequence 86-123.
Publication Date: 1976-06-01 PubMed ID: 62669DOI: 10.1002/eji.1830060607Google Scholar: Lookup
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  • Comparative Study
  • Journal Article

Summary

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The research is about identifying the regions in equine growth hormone that trigger an immune response. Certain fragments of the hormone, particularly those comprising specific amino acid sequences, were found to elicit this response.

Research Methodology

  • The study used peptide fragments from equine growth hormone, obtained through the process of cyanogen bromide cleavage and further chemical treatment.
  • These isolated fragments were then put through a series of tests to detect their immunological reactivities. This involved using hemagglutination and complement fixation methods with rabbit antisera against the native hormone.

Findings

  • The research found that antigenic determinants, parts of the hormone that trigger an immune response, were present in the fragments containing amino acid sequences 5-72 and 73-123, with the latter being more predominant.
  • On the other hand, the fragment with the sequence 124-178 showed very low reactivity, implying that this part of the hormone doesn’t play a significant role in activating an immune response.
  • The study also showed that the immunological properties of peptide 73-123 remained unchanged even after nitration, a chemical process that usually affects substances’ properties. However, oxidation caused a decrease in these properties, highlighting that the immune-triggering potential of this hormone fragment is susceptible to certain chemical changes.

Comparison with Ovine Growth Hormone

  • The antigenicity of the equine growth hormone fragment 73-123 was compared with the homologous ovine growth hormone fragment 86-123. This comparison suggested that at least one area in the horse hormone fragment that triggers an immune response depends on the sequence 86-123.
  • This finding suggests a degree of similarity between the two types of growth hormones, hinting at a possible common evolutionary derivation or a similar functional role.

Cite This Article

APA
Poskus E, Zakin MM, Fernámdez HN, Paladini AC. (1976). Detection of immunologically active zones in equine growth hormone. Eur J Immunol, 6(6), 409-417. https://doi.org/10.1002/eji.1830060607

Publication

ISSN: 0014-2980
NlmUniqueID: 1273201
Country: Germany
Language: English
Volume: 6
Issue: 6
Pages: 409-417

Researcher Affiliations

Poskus, E
    Zakin, M M
      Fernámdez, H N
        Paladini, A C

          MeSH Terms

          • Animals
          • Cyanogen Bromide
          • Epitopes
          • Growth Hormone / immunology
          • Horses
          • Oxidation-Reduction
          • Peptides / immunology
          • Sheep
          • Species Specificity
          • Structure-Activity Relationship

          Citations

          This article has been cited 1 times.
          1. Roguin LP, Delfino JM, Vita N, Paladini AC. Binding in vitro to rat liver receptors does not correlate with activities in vivo of bovine somatotropin. Use of chemically modified derivatives as probes. Biochem J 1984 Dec 1;224(2):535-40.
            doi: 10.1042/bj2240535pubmed: 6097223google scholar: lookup