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Intra‐ and Interchain Disulfide Bond Generation in S100b Protein
Author(s) -
Mely Yves,
Gérard Dominique
Publication year - 1990
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1990.tb03111.x
Subject(s) - disulfide bond , chemistry , monomer , redox , protein disulfide isomerase , thiol , ionic bonding , biophysics , ion , stereochemistry , biochemistry , organic chemistry , biology , polymer
Disulfide‐bridged S100b protein formation, air‐catalyzed and induced by thiol/disulfide exchange, was studied under various ionic conditions. As native, physiological disulfide‐bridged proteins are obtained easily from their reduced counterparts under appropriate redox conditions, this work was performed to determine whether this was the case for disulfide‐bridged S100b proteins, reported to have neurite extension activity. In nondenaturating native medium, no disulfide‐bridged species could be generated from reduced proteins in any of the ion‐induced conformations tested (no ions, Ca 2+ , Zn 2+ , or K + ) under widely different redox conditions. Only mixed disulfides accumulated, in certain cases. In contrast, intrasubunit monomeric and intersubunit dimeric disulfide‐bridged species were readily and efficiently generated under denaturating conditions. A brief characterization of these oxidized species suggested that they differed widely in structure from their reduced counterparts and that they probably did not bind Ca 2+ . Taken together, these data question the physiological relevance of these disulfide‐bridged S100b protein species.