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 language||English (US)|
|Number of pages||6|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - Jul 10 1974|
ASJC Scopus subject areas
- Molecular Biology