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The complete amino acid sequence of bovine spleen cathepsin S has been determined. The single-chain protein 217 residues and has a Mrof 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.

The complete amino acid sequence of bovine spleen cathepsin S has been determined. The single‐chain protein 217 residues and has a Mrof 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.