Subunit structure of wheat germ agglutinin

Robert H. Rice, Marilynn E. Etzler

Research output: Contribution to journalArticle

42 Scopus citations

Abstract

Wheat germ agglutinin was found to have a molecular weight of 36,200 ± 5% at pH 7.2 by high-speed sedimentation equilibrium. At this pH, the protein had a sedimentation coefficient of 3.5 S. These data indicate that the native agglutinin consists of dimers of the 18,000-dalton subunits observed upon sodium dodecyl sulfate polyacrylamide gel electrophoresis. Agglutinin treated with 0.05 N HCl, in which it sedimented at 2.1 S, and then dialyzed back to pH 7.2 sedimented as the native protein, suggesting reversible denaturation of the protein or dissociation of subunits.

Original languageEnglish (US)
Pages (from-to)414-419
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume59
Issue number1
DOIs
StatePublished - Jul 10 1974

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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