The complete primary structure of bovine stefin B

FEBS Letters

Turk, Boris¹  Križaj, Igor¹  Turk, Vito¹ 

[1] Department of Biochemistry, J. Stefan Institute, Jamova 39, 61000 Ljubljana, Slovenia, Yugoslavia

关键词: Stefin B;    Cystatin;    Cysteine proteinase inhibitor;    Primary structure;    CPI;    cysteine proteinase inhibitor;    CM;    carboxymethyl;    PE;    pyridylethyl;    TFA;    trifluoroacetic acid;    PP IV;    papaya proteinase IV;    HPLC;    high pressure liquid chromatography;    PTH;    phenyl-thio-hydantoin;    FAB;    fast atom bombardment;   

DOI  :  10.1016/0014-5793(92)80066-P

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A new stefin B-type low-M _r, CPI was isolated from bovine thymus and subjected to structural analysis. The inhibitor consisted of 98 amino acids and its M _r was calculated to be 11,178. The NH₂-terminal amino acid residue was blocked. The sequence was determined by automated sequencing of peptides derived by cleavage with cyanogen bromide and fragments of the inhibitor resulting from enzymatic digestion with β-trypsin and Staphylococcus aureus V-8 proteinase. The NH₂-terminal blocking group was established with mass spectrometry. The inhibitor exhibits considerable sequence homology with inhibitors from the stefin family. Furthermore, a highly conserved QVVAG region within the stefin family is for the first time replaced by the QLVAG sequence.

【 授权许可】

Unknown