https://www.selleckchem.com/pr....oducts/apo866-fk866.
Photolytic cleavage of disulfide bonds in proteins by UV light will influence their structure and functionality. The present study aimed to investigate the efficiency of disulfide cleavage by UV-B light in a system without a protein backbone consisting of combinations of cystine (a disulfide) and tryptophan (Trp) or tyrosine (Tyr) under anaerobic and aerobic conditions and to identify oxidation products formed by UV-B light. Cystine was reduced to cysteine (Cys) almost with a 11 stoichiometry by photoexcited Trp for anaerobic equim
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