Subunit structure of wheat germ agglutinin

Robert H. Rice, Marilynn E. Etzler

Research output: Contribution to journalArticlepeer-review

43 Scopus citations


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
Issue number1
StatePublished - Jul 10 1974

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology


Dive into the research topics of 'Subunit structure of wheat germ agglutinin'. Together they form a unique fingerprint.

Cite this