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.
Original language | English (US) |
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Pages (from-to) | 49-51 |
Number of pages | 3 |
Journal | FEBS Letters |
Volume | 279 |
Issue number | 1 |
DOIs | |
State | Published - Feb 11 1991 |
Externally published | Yes |
Keywords
- Bacterial protease
- Intrinsic fluoroscence
- Split actin
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology