Abstract
The subunit structure of canavalin was studied. The native protein has a sedimentation coefficient of 6.4 S and a MW of 91 000. SDS gel electrophoresis of the fully dissociated protein gave a single band, corresponding to a polypeptide chain with a MW of 22700. A minimal MW of 20700 was estimated from the amino acid composition. On a MW basis the native molecule consists of 4 chains. Support for the tetrameric structure of canavalin is provided by the electrophoretic pattern of partially dissociated protein.
Original language | English |
---|---|
Pages (from-to) | 1015-1016 |
Number of pages | 2 |
Journal | Phytochemistry |
Volume | 17 |
Issue number | 6 |
DOIs | |
State | Published - 1978 |
Keywords
- Canavalia ensiformis
- Leguminosae
- canavalin
- jack beans
- proteins.
- subunit structure