JOURNAL OF MOLECULAR BIOLOGY 317(1) 159-167 2002年3月
Solution structure of POIA1 (Pleurotus ostreatus proteinase A inhibitor 1), which functions as an intramolecular chaperone and as an inhibitor to subtilisin, was determined. By making use of the fact that POIA1 is the only structured protein that ...
JOURNAL OF MOLECULAR BIOLOGY 317(1) 159-167 2002年3月
Solution structure of POIA1 (Pleurotus ostreatus proteinase A inhibitor 1), which functions as an intramolecular chaperone and as an inhibitor to subtilisin, was determined. By making use of the fact that POIA1 is the only structured protein that ...
The propeptide of subtilisin BPN', which functions as an intramolecular chaperone and a temporary inhibitor of subtilisin, is unique in that it acquires its three-dimensional structure by formation of a complex with the cognate protease. We previo...
The propeptide of subtilisin BPN', which functions as an intramolecular chaperone and a temporary inhibitor of subtilisin, is unique in that it acquires its three-dimensional structure by formation of a complex with the cognate protease. We previo...
M Kitamura T Nakanishi S Kojima Kumagai, I H Inoue
JOURNAL OF BIOCHEMISTRY 129(3) 357-364 2001年3月
We identified a gene encoding a catalase from the anaerobic bacteria Desulfovibrio vulgaris (Miyazaki F), and the expression of its gene in Escherichia coli, The 3.3-kbp DNA fragment isolated from D. vulgaris (Miyazaki F) by double digestion with ...
人文科学研究科
理学部