Abstract
The complete amino acid sequence of bovine spleen cathepsin S has been determined. The single-chain protein 217 residues and has a Mr of 23 682. The primary structure was determined by sequencing of native protein and the peptides obtained by proteolytic cleavage with β-trypsin, papaya proteinase IV and by chemical cleavage with cyanogen bromide. Comparison of the amino terminal sequences of the heavy and the light chain of bovine cathepsin L with that of bovine cathepsin S clearly indicates that the enzymes are structurally different.
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