Literature DB >> 1515072

Isolation and characterization of bovine stefin B.

B Turk1, I Krizaj, V Turk.   

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.

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Year:  1992        PMID： 1515072     DOI： 10.1515/bchm3.1992.373.2.441

Source DB:  PubMed          Journal:  Biol Chem Hoppe Seyler        ISSN： 0177-3593


  2 in total

1.  The N-terminal region of cystatin A (stefin A) binds to papain subsequent to the two hairpin loops of the inhibitor. Demonstration of two-step binding by rapid-kinetic studies of cystatin A labeled at the N-terminus with a fluorescent reporter group.

Authors:  S Estrada; S T Olson; E Raub-Segall; I Björk
Journal:  Protein Sci       Date:  2000-11       Impact factor: 6.725

2.  Role of the single cysteine residue, Cys 3, of human and bovine cystatin B (stefin B) in the inhibition of cysteine proteinases.

Authors:  E Pol; I Björk
Journal:  Protein Sci       Date:  2001-09       Impact factor: 6.725
  2 in total

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