Physico-chemical properties of actin cleaved with bacterial protease from E. coli A2 strain.

Abstract:

: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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Khaitlina SYu,Collins JH,Kuznetsova IM,Pershina VP,Synakevich IG,Turoverov KK,Usmanova AM

doi

10.1016/0014-5793(91)80247-z

subject

Has Abstract

pub_date

1991-02-11 00:00:00

pages

49-51

issue

1

eissn

0014-5793

issn

1873-3468

journal_volume

279

pub_type

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