The amino acid sequence around the active-site cysteine and histidine residues of stem bromelain

Author:

Husain S. S.1,Lowe G.1

Affiliation:

1. The Dyson Perrins Laboratory, University of Oxford, Oxford OX1 3QY, U.K.

Abstract

Stem bromelain that had been irreversibly inhibited with 1,3-dibromo[2-14C]-acetone was reduced with sodium borohydride and carboxymethylated with iodoacetic acid. After digestion with trypsin and α-chymotrypsin three radioactive peptides were isolated chromatographically. The amino acid sequences around the cross-linked cysteine and histidine residues were determined and showed a high degree of homology with those around the active-site cysteine and histidine residues of papain and ficin.

Publisher

Portland Press Ltd.

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