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The complete primary structure of bovine stefin B
Author(s) -
Križaj Igor,
Turk Boris,
Turk Vito
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80066-p
Subject(s) - cyanogen bromide , peptide sequence , protein primary structure , chemistry , trypsin , biochemistry , residue (chemistry) , cleavage (geology) , complete sequence , amino acid , trypsin inhibitor , sequence (biology) , enzyme , microbiology and biotechnology , biology , paleontology , genome , fracture (geology) , gene
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 NH 2 ‐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 NH 2 ‐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.