Open AccessAmino acid sequence of a 12‐kDa inhibitor of protein kinase C
Author(s) -
MOZIER Ned M.,
ZÜRCHERNEELY Heidi A.,
GUIDO David M.,
MATHEWS W. Rodney,
HEINRIKSON Robert L.,
FRASER Elaine D.,
WALSH Michael P.,
PEARSON James D.
Publication year - 1990
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1990.tb19421.x
Subject(s) - edman degradation , cyanogen bromide , peptide sequence , protein primary structure , chymotrypsin , trypsin , chemistry , protease , biochemistry , amino acid , molecular mass , fast atom bombardment , cleavage (geology) , trypsin inhibitor , sequence (biology) , microbiology and biotechnology , mass spectrometry , biology , enzyme , chromatography , paleontology , fracture (geology) , gene
The complete primary structure of a bovine‐brain‐derived inhibitor of protein kinase C has been established. Fragments of the purified protein were obtained by cleavage with cyanogen bromide, Staphylococcus aureus V8 protease, trypsin and chymotrypsin. Subsequent analysis of the resulting fragments by fast‐atom‐bombardment mass spectrometry and Edman degradation revealed a calculated molecular mass of 11779 Da with the following 107‐amino‐acid sequence:This inhibitor does not share significant primary structural identity with any other known protein.