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The Complexing of Concanavalin A and Glucans
Author(s) -
Erlander Stig R.
Publication year - 1970
Publication title -
starch ‐ stärke
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.62
H-Index - 82
eISSN - 1521-379X
pISSN - 0038-9056
DOI - 10.1002/star.19700220909
Subject(s) - carboxylate , tetramer , chelation , concanavalin a , chemistry , folding (dsp implementation) , molecule , ion , mannose , stereochemistry , medicinal chemistry , inorganic chemistry , biochemistry , organic chemistry , enzyme , electrical engineering , in vitro , engineering
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 of various glucans again illustrates that C‐6 and C‐4 hydroxyls must be involved in the complexing 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, if 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 change in pK and inactivation of these groups.