Quantitative polyacrylamide gel electrophoresis and specific activities of human somatotropin and its derivatives

Jay S. Skyler, Andreas Chrambach, Choh Hao Li

Research output: Contribution to journalArticle

4 Scopus citations

Abstract

A preparation of human pituitary somatotropin examined in quantitative polyacrylamide gel electrophoresis is conformationally compact. The derived molecular weight by quantitative electrophoresis is consistent with the known mass of the hormone and values obtained by other methods. A plasmin modified somatotropin is more compact and shows full activity in immunoassay, and in lymphocyte binding and somatotropic assays, with enhanced lactogenic activity. The N terminal 134 amino acid fragment and a hendekakaihekaton fragment exist in non monometric forms. The N terminal fragment has immunologic and biologic activity, with greatest activity in the in vivo somatotropic assay. The hendekakaihekaton fragment exhibited only marginal activity. All preparations showed heterogeneity of charge in quantitative electrophoresis with discrete charge isomerism recognizable for the native and plasmin modified preparations.

Original languageEnglish (US)
Pages (from-to)566-572
Number of pages7
JournalBBA - Protein Structure
Volume491
Issue number2
DOIs
StatePublished - Apr 25 1977
Externally publishedYes

ASJC Scopus subject areas

  • Medicine(all)

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