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Subtilisin carlsberg III. isolation and amino acid composition of chymotryptic peptides

By Michael Landon, William Howard Evans and Emil L. Smith

Abstract

From a chymotryptic digest of diisopropylphosphoryl subtilisin Carlsberg, 44 peptides were isolated by fractionation on a column of Dowex 50, followed by purification by various methods. The amino acid compositions of these peptides are reported. The peptides account for 272 of the 274 residues present in the single peptide chain of this protein. Six of the peptides represented segments of incomplete hydrolysis by chymotrypsin

Topics: R1
Publisher: American Society for Biochemistry and Molecular Biology
Year: 1968
OAI identifier: oai:http://orca.cf.ac.uk:66368
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