Isolation and characterization of bovine stefin B

Biol Chem Hoppe Seyler. 1992 Jul;373(7):441-6. doi: 10.1515/bchm3.1992.373.2.441.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cattle
  • Chromatography, DEAE-Cellulose
  • Chromatography, Gel
  • Chromatography, Ion Exchange
  • Cystatin B
  • Cystatins / analysis
  • Cystatins / isolation & purification*
  • Electrophoresis, Polyacrylamide Gel
  • Isoelectric Focusing
  • Molecular Sequence Data
  • Thymus Gland / chemistry*


  • Cystatins
  • Cystatin B