PMID: 4898282Sep 1, 1969Paper

Completion of the amino acid sequence of papain

The Biochemical Journal
S S Husain, G Lowe

Abstract

Papain was inhibited with bromo[2-(14)C]acetic acid, the tertiary structure of the inhibited enzyme was unfolded and the disulphide bridges were reduced with mercaptoethanol and aminoethylated. Digestion with trypsin gave a radioactive peptide consisting of residues 18-58 inclusive and containing therefore the sequence of the thirteen unknown residues 29-41 in the primary sequence of papain. This peptide was digested with pepsin to give a radioactive peptide consisting of residues 18-47, which after digestion with 0.4m-hydrochloric acid gave a radioactive peptide consisting of residues 24-43 inclusive. Further digestion with 6m-hydrochloric acid gave peptides that were used to determine the sequence: Ser-Ala-Val-Val-Thr-Ile-Glx-Gly-Ile-Ile-Lys-Ile-Arg for the residues 29-41, so completing the amino acid sequence of papain.

Citations

Nov 1, 1971·Photochemistry and Photobiology·G Jori, G Galiazzo
Jan 1, 1972·Photochemistry and Photobiology·K Dose, S Risi
Feb 21, 1989·Biochemistry·I BjörkK Ylinenjärvi
Jan 12, 1993·Biochemistry·B TurkJ G Bieth
Oct 23, 1970·Biochemical and Biophysical Research Communications·B Weinstein
Sep 15, 1995·The Journal of Biological Chemistry·I DolencV Turk
Dec 9, 2004·Chemical Reviews·Dave R van Staveren, Nils Metzler-Nolte
Apr 14, 1971·Biochimica Et Biophysica Acta·D M Kirschenbaum
Mar 1, 1972·Archives of Biochemistry and Biophysics·B Friedenson, I E Liener
Mar 14, 1972·Journal of Molecular Biology·A D McLachlan

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