作者: Ronald E.J. Mitchel , Irwin M. Chaiken , Emil L. Smith
DOI: 10.1016/S0021-9258(18)62954-0
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摘要: Abstract The active cysteine of papain was labeled with 14C-iodoacetate and the cystine residues were reduced coupled unlabeled iodoacetate. heptacarboxymethyl then maleyalated hydrolyzed trypsin. Key peptides isolated from this hydrolysate which have permitted completion amino acid sequence protein. Thus, an earlier tentative incomplete version has been corrected shown to be in accord studies Drenth et al. (Drenth, J., Jansonius, J. N., Koekoek, R., Swen, H. M., Wolthers, B. G., Nature, 218, 929 (1968)) by x-ray crystallographic methods.