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Dilute Acid Hydrolysis Of Papain. Kinetic Studies And Peptides From The Carboxymethylated Protein

, : Dilute Acid Hydrolysis Of Papain. Kinetic Studies And Peptides From The Carboxymethylated Protein. Journal of Biological Chemistry 240: 281-289

Kinetic studies of the release of free amino acids from S-carboxymethyl papain in dilute HC1 were performed with the aid of the automatic amino acid analyzer. Aspartic acid was released more rapidly than any other amino acid, but there was no change in selectivity with changing concentration of HC1. A partial acid hydrolysate of S-carboxymethyl papain was resolved into 90 fractions by gradient elution chromatography on a column of Dowex 50-X2. Some peptides, isolated by various procedures, proved to be extensions of known sequences and established a number of overlapping sequences. Other peptides were useful for confirmation or correction of previous sequence studies. From these peptides it was evident that extensive hydrolysis occurred at peptide bonds vicinal to aspartic acid and, in addition, at residues of glutamic acid, glycine, alanine, serine, and threonine. The yields of isolated peptides averaged below 10%.


PMID: 14253425

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