Abstract
Previous studies were interpreted as showing that transition metal and calcium ions must be bound to concanavalin A before this lectin can bind sugars. In contrast, it was found that the addition of calcium ions fails to affect the following properties of manganese concanavalin A if the metalloprotein is prepared in their presence: electron spin resonance spectrum of the manganese ion in the protein; spin lattice relaxation time of solvent water protons measured in the presence of the protein; and spin lattice and transverse relaxation times of the 13C carbons of α methyl D glucopyranoside (uniformly enriched with 14% 13C) in the presence of manganese concanavalin A. These results indicate that saccharide binding activity of the protein is independent of calcium ion binding if a transition metal ion (Mn2+) initially binds to the protein in the presence of calcium ions. The role of calcium ion binding to concanavalin A appears to be that of accelerating the rate of formation of the final transition metal protein complex.
Original language | English (US) |
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Pages (from-to) | 4614-4616 |
Number of pages | 3 |
Journal | Journal of Biological Chemistry |
Volume | 249 |
Issue number | 14 |
State | Published - 1974 |
Externally published | Yes |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology