Physico-chemical properties of actin cleaved with bacterial protease from E. coli A2 strain.
The 36 kDa fragment of actin molecule obtained with the protease from E. coli A2 strain [(1988) FEBS Lett. 228, 172] was shown to begin with Val-43 and retain the COOH-terminal amino acid residues of the parent molecule. The E. coli protease split actin preserves the NH2-terminal part of the polypeptide chain as well as the native conformation of actin molecule. However, the E. coli protease split actin failed to polymerize in 0.1 M KCl, suggesting that integrity of actin molecule between Gly-42 and Val-43 is crucial for actin polymerization.
Khaitlina SYu
Institute of Cytology, USSR Academy of Sciences, Leningrad.
Collins
J H
JH
Kuznetsova
I M
IM
Pershina
V P
VP
Synakevich
I G
IG
Turoverov
K K
KK
Usmanova
A M
AM
D000199:Actins / Q000737:chemistry*; D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology*; D006868:Hydrolysis; D011817:Rabbits; D013045:Species Specificity; D013050:Spectrometry, Fluorescence
D000199:Actins; D010450:Endopeptidases