M Oda   A Tamura   K Kanaori   S Kojima   K Miura   K Momma   B Tonomura   K Akasaka   
JOURNAL OF BIOCHEMISTRY 132(6) 991-995 2002年12月
Single amino acid mutations of Met103 in the hydrophobic core of a serine protease inhibitor, Streptomyces subtilisin inhibitor, caused little change in the inhibitory activity, as measured by the inhibitor constant, although some altered the ther...
M Motizuki   T Satoh   T Takei   T Itoh   S Yokota   S Kojima   K Miura   T Samejima   K Tsurugi   
JOURNAL OF BIOCHEMISTRY 132(1) 115-119 2002年7月
We previously showed that bovine apolipoprotein A-II (apoA-II) has antimicrobial activity against Escherichia coli in PBS, and its C-terminal residues 49-76 are responsible for the activity using synthetic peptides. In order to understand the stru...
Pleurotus ostreatus proteinase A inhibitor 1 (POIA1) has been shown to be unique among the various serine protease inhibitors in that its C-terminal region appears to be the reactive site responsible for its inhibitory action toward proteases. To ...
Pleurotus ostreatus proteinase A inhibitor 1 (POIA1) has been shown to be unique among the various serine protease inhibitors in that its C-terminal region appears to be the reactive site responsible for its inhibitory action toward proteases. To ...