## Abstract (1) Membrane vesicles from rabbit thymocytes accumulate α‐aminoisobutyrate in the presence of 0.1 M NaCl. Uptake is 1/2 maximal after about 2 min and reaches a plateau value (61 pmoles/mg protein) after 30 min. (2) Up to 25 μg concanavalin A/ml, binding of the lectin describes a sigmoid
Low- and high-affinity concanavalin A binding to thymocyte plasma membrane vesicles
✍ Scribed by Donald F. H. Wallach; Rupert Schmidt-Ullrich
- Book ID
- 102309250
- Publisher
- John Wiley and Sons
- Year
- 1976
- Tongue
- English
- Weight
- 257 KB
- Volume
- 89
- Category
- Article
- ISSN
- 0021-9541
No coin nor oath required. For personal study only.
✦ Synopsis
Abstract
Binding of concanavalin A to isolated thymocyte membrane vesicles occurs through (a) numerous (∼6 × 10^6^/cell equivalent) low‐affinity sites (K~a~ = 1.3 × 10^5^ M^−1^) and (b) fewer (∼0.4 × 10^6^/cell equipment) specific receptors (K~a~ = 6.8 × 10^6^ M^−1^) defined as 55,000 D glycoprotein and its multimers. Specific binding is positively‐cooperative, with a Hill coefficient of∼1.8. Low concentrations of glutaraldehyde selectively crosslink the 55,000 D glycoprotein with replacement of positively‐cooperative sites by high‐affinity sites. It is proposed that concanavalin A‐binding induces multimerization of the 55,000 D glycoprotein.
📜 SIMILAR VOLUMES
## Abstract Binding of Concanavalin A to mouse L cells which were grown in serum free, chemically defined medium and depleted of their membrane sterol by blocking their de novo sterol synthesis was investigated. Kinetic analysis of binding data implied positive cooperativity, with two different aff