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“Treatment of such vesicles with papain gave rise to further cleavages of the polypeptide localized between 30 and 31, 186 and 187 amino acid residues.”
European journal of biochemistry • 1984 | View Paper
“We have been using proteolytic enzymes to study the topography of the outer segment membranes, and report here that papain rapidly removes one third of the polypeptide chain of rhodopsin, leaving a residue whose spectral properties are unchanged.”
“This polypeptide is an inhibitor of papain and other cysteine proteinases and is capable of binding several proteinase molecules simultaneously (P. Rodis, J.E. Hoff [1984] Plant Physiol 74: 907–911).”