Protein Inhibitors of Cysteine Proteinases. I. Isolation and Characterization of Stefin, a Cytosolic Protein Inhibitor of Cysteine Proteinases from Human Polymorphonuclear Granulocytes
- 1 January 1983
- journal article
- research article
- Published by Walter de Gruyter GmbH in Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie
- Vol. 364 (2), 1475-1480
- https://doi.org/10.1515/bchm2.1983.364.2.1475
Abstract
A protein inhibitor of cysteine proteinases, stefin, was purified from cytosol of human polymorphonuclear granulocytes. Affinity chromatography on carboxymethylated papain-Sepharose was used as the 1st step, followed by ion exchange chromatography on DEAE-Sephacel, which resolved 4 inhibitory peaks. The main peak, comprising .apprx. 80% of total inhibitory activity was characterized. It was found to be a homogenous protein with an apparent molecular mass slightly lower than that of cytochrome c and with an isoelectric point of 4.65. The inhibitor inhibits papain at a molar ratio of 1:1 as well as cathepsin B and H, but it does not inhibit serine and aspartic proteinases. It is stable at elevated temperature and in alkaline pH, but looses its activity in acid pH. Oxidized glutathione has no effect on it inhibitory activity.This publication has 20 references indexed in Scilit:
- Cerebrocystatin suppresses degradation of myelin basic protein by purified brain cysteine proteinaseBiochemical and Biophysical Research Communications, 1983
- Isolation and immunological studies of high and low molecular weight cysteine proteinase inhibitors in bovine serumBiochimica et Biophysica Acta (BBA) - General Subjects, 1983
- Protein Inhibitors of Cysteine Proteinases. II. Primary Structure of Stefin, a Cytosolic Protein Inhibitor of Cysteine Proteinases from Human Polymorphonuclear GranulocytesHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1983
- A heat stable low molecular weight inhibitor of lysosomal cysteine proteinases in human serumBiochemical and Biophysical Research Communications, 1983
- Protein Inhibitors of Cysteine Proteinases. III. Amino-Acid Sequence of Cystatin from Chicken Egg WhiteHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1983
- Low molecular weight inhibitors of cathepsins B, H and T in human serum, synovial fluid and CSFBiochemical and Biophysical Research Communications, 1982
- Further characterization of cysteine proteinase inhibitors purified from rat and human epidermisBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982
- Isolation and partial characterisation of a thiol proteinase inhibitor from human plasmaBiochemical and Biophysical Research Communications, 1979
- A new serum component which specifically inhibits thiol proteinasesBiochemical and Biophysical Research Communications, 1977
- The preparation and properties of two new chromogenic substrates of trypsinArchives of Biochemistry and Biophysics, 1961