Physico‐chemical properties of actin cleaved with bacterial protease from E. coli A2 strain
1991; Wiley; Volume: 279; Issue: 1 Linguagem: Inglês
10.1016/0014-5793(91)80247-z
ISSN1873-3468
AutoresSofia Khaitlina, John H. Collins, Irina М. Kuznetsova, V.P. Pershina, I.G. Synakevich, Konstantin К. Turoverov, A.M. Usmanova,
Tópico(s)Protein Interaction Studies and Fluorescence Analysis
ResumoThe 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.
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