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• W2041020439 abstract "Disulfide-bridged S100b protein formation, aircatalyzed 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, Ca2+, Zn2+, 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 Ca2+. Taken together, these data question the physiological relevance of these disulfide-bridged S100b protein species." @default.
• W2041020439 created "2016-06-24" @default.
• W2041020439 creator A5046440030 @default.
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• W2041020439 date "1990-10-01" @default.
• W2041020439 modified "2023-09-26" @default.
• W2041020439 title "Intra- and Interchain Disulfide Bond Generation in S100b Protein" @default.
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• W2041020439 doi "https://doi.org/10.1111/j.1471-4159.1990.tb03111.x" @default.
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