Protein inhibitors of cysteine proteinases. II. Primary structure of stefin, a cytosolic protein inhibitor of cysteine proteinases from human polymorphonuclear granulocytes. 1983

W Machleidt, and U Borchart, and H Fritz, and J Brzin, and A Ritonja, and V Turk

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.

UI MeSH Term Description Entries
D008970 Molecular Weight The sum of the weight of all the atoms in a molecule. Molecular Weights,Weight, Molecular,Weights, Molecular
D009504 Neutrophils Granular leukocytes having a nucleus with three to five lobes connected by slender threads of chromatin, and cytoplasm containing fine inconspicuous granules and stainable by neutral dyes. LE Cells,Leukocytes, Polymorphonuclear,Polymorphonuclear Leukocytes,Polymorphonuclear Neutrophils,Neutrophil Band Cells,Band Cell, Neutrophil,Cell, LE,LE Cell,Leukocyte, Polymorphonuclear,Neutrophil,Neutrophil Band Cell,Neutrophil, Polymorphonuclear,Polymorphonuclear Leukocyte,Polymorphonuclear Neutrophil
D010446 Peptide Fragments Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques. Peptide Fragment,Fragment, Peptide,Fragments, Peptide
D011480 Protease Inhibitors Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES). Antiprotease,Endopeptidase Inhibitor,Endopeptidase Inhibitors,Peptidase Inhibitor,Peptidase Inhibitors,Peptide Hydrolase Inhibitor,Peptide Hydrolase Inhibitors,Peptide Peptidohydrolase Inhibitor,Peptide Peptidohydrolase Inhibitors,Protease Antagonist,Protease Antagonists,Antiproteases,Protease Inhibitor,Antagonist, Protease,Antagonists, Protease,Hydrolase Inhibitor, Peptide,Hydrolase Inhibitors, Peptide,Inhibitor, Endopeptidase,Inhibitor, Peptidase,Inhibitor, Peptide Hydrolase,Inhibitor, Peptide Peptidohydrolase,Inhibitor, Protease,Inhibitors, Endopeptidase,Inhibitors, Peptidase,Inhibitors, Peptide Hydrolase,Inhibitors, Peptide Peptidohydrolase,Inhibitors, Protease,Peptidohydrolase Inhibitor, Peptide,Peptidohydrolase Inhibitors, Peptide
D011506 Proteins Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein. Gene Products, Protein,Gene Proteins,Protein,Protein Gene Products,Proteins, Gene
D003488 Cyanogen Bromide Cyanogen bromide (CNBr). A compound used in molecular biology to digest some proteins and as a coupling reagent for phosphoroamidate or pyrophosphate internucleotide bonds in DNA duplexes. Bromide, Cyanogen
D003600 Cytosol Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components. Cytosols
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D015891 Cystatins A homologous group of endogenous CYSTEINE PROTEINASE INHIBITORS. The cystatins inhibit most CYSTEINE ENDOPEPTIDASES such as PAPAIN, and other peptidases which have a sulfhydryl group at the active site. Cystatin,Cystatin Superfamily,Stefin,Cystatin-Related Proteins,Stefins,Type 1 Cystatins,Type 2 Cystatins,Type 3 Cystatins,Type I Cystatins,Type II Cystatins,Type III Cystatins,Cystatin Related Proteins,Cystatins, Type 1,Cystatins, Type 2,Cystatins, Type 3,Cystatins, Type I,Cystatins, Type II,Cystatins, Type III

Related Publications

W Machleidt, and U Borchart, and H Fritz, and J Brzin, and A Ritonja, and V Turk
November 1983, Hoppe-Seyler's Zeitschrift fur physiologische Chemie,
W Machleidt, and U Borchart, and H Fritz, and J Brzin, and A Ritonja, and V Turk
February 1995, FEBS letters,
W Machleidt, and U Borchart, and H Fritz, and J Brzin, and A Ritonja, and V Turk
October 1993, FEBS letters,
W Machleidt, and U Borchart, and H Fritz, and J Brzin, and A Ritonja, and V Turk
October 1989, FEBS letters,
W Machleidt, and U Borchart, and H Fritz, and J Brzin, and A Ritonja, and V Turk
September 1990, FEBS letters,
W Machleidt, and U Borchart, and H Fritz, and J Brzin, and A Ritonja, and V Turk
July 1991, Biochimica et biophysica acta,
W Machleidt, and U Borchart, and H Fritz, and J Brzin, and A Ritonja, and V Turk
January 1985, Progress in clinical and biological research,
W Machleidt, and U Borchart, and H Fritz, and J Brzin, and A Ritonja, and V Turk
July 1991, FEBS letters,
W Machleidt, and U Borchart, and H Fritz, and J Brzin, and A Ritonja, and V Turk
May 1988, Biological chemistry Hoppe-Seyler,
W Machleidt, and U Borchart, and H Fritz, and J Brzin, and A Ritonja, and V Turk
May 1990, Biological chemistry Hoppe-Seyler,
Copied contents to your clipboard!