Isolation and Characterization of Bovine Stefin B
- 1 January 1992
- journal article
- Published by Walter de Gruyter GmbH in Biological Chemistry Hoppe-Seyler
- Vol. 373 (2) , 441-446
- https://doi.org/10.1515/bchm3.1992.373.2.441
Abstract
A new cysteine proteinase inhibitor (CPI) was isolated from bovine thymus. According to the amino acid sequence it belongs to the stefin family. It appears as a monomer and a dimer with monomer M(r) of 11,178 and pI values 5.6 for the monomer and 5.2 and 5.6 for the dimer. Ki for the interaction with papain was determined to be 0.12 nM. The most interesting feature of bovine stefin B is the replacement of the highly conserved QVVAG region in stefins with the QLVAG sequence without interfering its inhibitory properties.This publication has 8 references indexed in Scilit:
- Evolution of proteins of the cystatin superfamilyJournal of Molecular Evolution, 1990
- Inhibitorily Active Recombinant Human Stefin B. Gene Synthesis, Expression and Isolation of an Inhibitorily Active MS-2 pol-Stefin B Fusion Protein and Preparation of Des[Met1,22] stefin BBiological Chemistry Hoppe-Seyler, 1988
- Amino acid sequence of the intracellular cysteine proteinase inhibitor cystatin B from human liverBiochemical and Biophysical Research Communications, 1985
- Amino acid sequence of rat epidermal thiol proteinase inhibitorBiochemical and Biophysical Research Communications, 1984
- Amino acid sequence of rat liver thiol proteinase inhibitorBiochemical and Biophysical Research Communications, 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
- [41] Cathepsin B, cathepsin H, and cathepsin LPublished by Elsevier ,1981