dc.contributor.author |
Itskovich E. |
|
dc.contributor.author |
Balaban N. |
|
dc.contributor.author |
Mardanova A. |
|
dc.contributor.author |
Shakirov E. |
|
dc.contributor.author |
Sharipova M. |
|
dc.contributor.author |
Leshchinskaya I. |
|
dc.contributor.author |
Ksenofontov A. |
|
dc.contributor.author |
Rudenskaya G. |
|
dc.date.accessioned |
2018-09-17T20:08:37Z |
|
dc.date.available |
2018-09-17T20:08:37Z |
|
dc.date.issued |
1997 |
|
dc.identifier.issn |
0006-2979 |
|
dc.identifier.uri |
https://dspace.kpfu.ru/xmlui/handle/net/133092 |
|
dc.description.abstract |
Effects of a thiol-dependent serine proteinase of Bacillus intermedius on peptide substrates and insulin B-chain were studied. The enzyme preferably splits peptide bonds formed by carboxyl groups of hydrophobic amino acids. Ca2+ increases the thermal stability of the proteinase significantly. The kinetic characteristics of hydrolysis of Z-Ala-Ala-Leu-pNA by this enzyme was determined as Km = 1.25 mM and kcat = 0.15 sec-1. The enzyme has high stability to DMFA and isopropanol, and is able to catalyze peptide bond synthesis. |
|
dc.relation.ispartofseries |
Biochemistry (Moscow) |
|
dc.subject |
Enzymatic synthesis of substrates |
|
dc.subject |
Substrate specificity |
|
dc.subject |
Thiol-dependent serine proteinase |
|
dc.title |
Enzymatic properties of thiol-dependent serine proteinase of Bacillus intermedius 3-19 |
|
dc.type |
Article |
|
dc.relation.ispartofseries-issue |
1 |
|
dc.relation.ispartofseries-volume |
62 |
|
dc.collection |
Публикации сотрудников КФУ |
|
dc.relation.startpage |
49 |
|
dc.source.id |
SCOPUS00062979-1997-62-1-SID0030642217 |
|