The interaction of cr-D-glucans with Concanavalin A has been studied by turbidimetry. Amylopectins from various botanical sources and two glycogens were characterised for their fine structure [% (1-+6)-a-linkages, % beta-amylolysis, iodine interaction] and their molecular size (intrinsic viscosity,
The Complexing of Concanavalin A and Glucans
β Scribed by Stig R. Erlander
- Book ID
- 104599678
- Publisher
- John Wiley and Sons
- Year
- 1970
- Tongue
- English
- Weight
- 351 KB
- Volume
- 22
- Category
- Article
- ISSN
- 0038-9056
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β¦ Synopsis
The complex between concanavalin A and glucans was again analyzed with respect to the recent results reported by Doyle. A discussion of the complexing behavior o f various glucans again illustrates that C-6 and C-4 hydroxyls must be involved in the cornplexing mechanism. Carboxylate groups are most likely not involved in the complex, because 4.2 M NaCl can not prevent the complex from forming. That is, i f carboxylate ions were involved, such concentrated Na+ ions would act as inhibitors to the reaction with more strength than neutral molecules such as D-mannose. Carboxylate groups are most likely chelated to Mn++ ions and hence are involved in the stabilization of the protein tetramer. Such complexing as well as the folding of the protein could account for changes in pK and inactivation of these groups.
π SIMILAR VOLUMES
A molecular model for the complex formed between the jack bean lectin concanavalin A (Con A) and glycopeptides of the complex biantennary class is described. The model was derived using coordinate: for Con A determined by x-ray crystallographic refinement techniques, with 1.75-A resolution data, and