dc.contributor.author |
Khaitlina S. |
|
dc.contributor.author |
Collins J. |
|
dc.contributor.author |
Kuznetsova I. |
|
dc.contributor.author |
Pershina V. |
|
dc.contributor.author |
Synakevich I. |
|
dc.contributor.author |
Turoverov K. |
|
dc.contributor.author |
Usmanova A. |
|
dc.date.accessioned |
2018-09-17T20:12:37Z |
|
dc.date.available |
2018-09-17T20:12:37Z |
|
dc.date.issued |
1991 |
|
dc.identifier.issn |
0014-5793 |
|
dc.identifier.uri |
https://dspace.kpfu.ru/xmlui/handle/net/133185 |
|
dc.description.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. © 1991. |
|
dc.relation.ispartofseries |
FEBS Letters |
|
dc.subject |
Bacterial protease |
|
dc.subject |
Intrinsic fluoroscence |
|
dc.subject |
Split actin |
|
dc.title |
Physico-chemical properties of actin cleaved with bacterial protease from E. coli A2 strain |
|
dc.type |
Article |
|
dc.relation.ispartofseries-issue |
1 |
|
dc.relation.ispartofseries-volume |
279 |
|
dc.collection |
Публикации сотрудников КФУ |
|
dc.relation.startpage |
49 |
|
dc.source.id |
SCOPUS00145793-1991-279-1-SID0026079005 |
|