Protein inhibitors of cysteine proteinases. II. Primary structure of stefin, a cytosolic protein inhibitor of cysteine proteinases from human polymorphonuclear granulocytes.
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.
D000595:Amino Acid Sequence; D003488:Cyanogen Bromide; D055313:Cystatin B; D015891:Cystatins; D003600:Cytosol / Q000378:metabolism; D006801:Humans; D008970:Molecular Weight; D009504:Neutrophils / Q000201:enzymology*; D010446:Peptide Fragments / Q000032:analysis; D011480:Protease Inhibitors / Q000302:isolation & purification*; D011506:Proteins / Q000302:isolation & purification*
C524994:CSTB protein, human; D015891:Cystatins; D010446:Peptide Fragments; D011480:Protease Inhibitors; D011506:Proteins; D055313:Cystatin B; D003488:Cyanogen Bromide