Protein Inhibitors of Cysteine Proteinases. II. Primary Structure of Stefin, a Cytosolic Protein Inhibitor of Cysteine Proteinases from Human Polymorphonuclear Granulocytes

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Abstract
The primary structure of stefin, a new cysteine proteinase inhibitor from the cytosol of human polymorphonuclear granulocytes, was determined by amino-acid sequence analysis. The protein consists of 98 amino-acid residues and contains no cysteine Its molecular mass was calculated to be 11,006 Da [daltons]. The sequence was obtained by automatic solid-phase Edman degradation of the uncleaved protein and its cyanogen bromide fragments. There is no striking evidence for a sequence homology with known families of protein inhbitors of proteinases.