Premium
Physico‐chemical properties of actin cleaved with bacterial protease from E. coli A2 strain
Author(s) -
Khaitlina S.Yu.,
Collins J.H.,
Kuznetsova I.M.,
Pershina V.P.,
Synakevich I.G.,
Turoverov K.K.,
Usmanova A.M.
Publication year - 1991
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(91)80247-z
Subject(s) - strain (injury) , protease , chemistry , actin , bacterial strain , microbiology and biotechnology , bacteria , biophysics , biochemistry , enzyme , biology , genetics , anatomy
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 NH 2 ‐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.