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 11006 Da. 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 inhibitors of proteinases.

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