Literature DB >> 1238375

Selective reduction and alkylation of the COOH-terminal disulfide bridge in bovine growth hormone.

L Gráf, C H Li, T A Bewley.   

Abstract

Conditions leading to the cleavage of both disulfide bridges in human growth hormone caused the reduction of only one disulfide bond in bovine growth hormone. Partially reduced and alkylated derivatives of bovine growth hormone were prepared and characterized. It was shown that the reduction and alkylation modified the COOH-terminal disulfide bond, however, this modification does not result in the dissociation of the dimeric form of bovine growth hormone or cause a significant loss of growth-promoting activity.

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Year:  1975        PMID: 1238375     DOI: 10.1111/j.1399-3011.1975.tb02467.x

Source DB:  PubMed          Journal:  Int J Pept Protein Res        ISSN: 0367-8377


  3 in total

1.  Structural characterization of the two refold dimers of recombinant bovine somatotropin (bST).

Authors:  J S Tou; B N Violand; M R Schlittler; M G Jennings
Journal:  J Protein Chem       Date:  1993-04

2.  Extraordinarily stable disulfide-linked homodimer of human growth hormone.

Authors:  Alexei L Grigorian; Juan J Bustamante; Peter Hernandez; Andrew O Martinez; Luis S Haro
Journal:  Protein Sci       Date:  2005-03-01       Impact factor: 6.725

3.  Covalent cross-linking of the bovine somatotropin dimer. Effects on growth-promoting, receptor-binding and immunological activities and preliminary characterization of the self-association.

Authors:  H N Fernández; J M Delfino
Journal:  Biochem J       Date:  1983-01-01       Impact factor: 3.857

  3 in total

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