Abstract
Concanavalin A (Con A) was dissociated into dimeric and monomeric subunits by incubation at 37°C in acetate buffer of pH 3.8 containing 0.5% sodium dodecyl sulfate. The dimer was isolated in pure form by a density gradient ultracentrifugation method. Several properties of the dimer were determined including the formation of a precipitin with anti-Con A antibodies, the molecular weight, the lack of a binding site for glycogen, the lack of mitogenic activity for spleen lymphocytes, and the lack of inhibition by α-methyl D-glucoside. The latter findings differ from results reported by other investigators.
Original language | English (US) |
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Pages (from-to) | 353-359 |
Number of pages | 7 |
Journal | Journal of Protein Chemistry |
Volume | 19 |
Issue number | 5 |
DOIs | |
State | Published - 2000 |
All Science Journal Classification (ASJC) codes
- Biochemistry