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dc.contributor.author | Kutyreva M. | |
dc.contributor.author | Ulakhovich N. | |
dc.contributor.author | Gataulina A. | |
dc.contributor.author | Mukhametzyanova A. | |
dc.contributor.author | Khaldeeva E. | |
dc.date.accessioned | 2018-09-18T20:26:39Z | |
dc.date.available | 2018-09-18T20:26:39Z | |
dc.date.issued | 2013 | |
dc.identifier.issn | 1818-4952 | |
dc.identifier.uri | https://dspace.kpfu.ru/xmlui/handle/net/139938 | |
dc.description.abstract | The aim of work is to estimate ion Zn(II) influence on catalytic activity of secreted aspartic proteinase Candida albicans (SAP2). System ZnCl2 - SAP2 showed complex formation. Composition of [ZnmSAP2n] complex was 1:1, the stability constant was 4.73±0.20. Affinity constants in system SAP2 - human serum albumin (HSA) - ZnCl2 were determined at Skatchard coordinates. The SAP2 was found to have a one section for linking with the substrate and one section for linking with modulator. The affinity constants in SAP2 - HSA system decreased in presence of ZnCl2. Complex forming of SAP2 - ZnCl2 system resulted in reduction of enzyme-substrate bonding. Proteolytic activity of SAP2 towards HSA at presence ZnCl2 as modulator was estimated. The inhibition effect in range 1×10-4 - 4×10-6 and 6×10-7 - 1×10-8 M was observed. The SAP2 activation effect catalyzed by ZnCl2 at 5×10-7 - 5×10-6 M concentrations were fixed for the first time. © IDOSI Publications, 2013. | |
dc.relation.ispartofseries | World Applied Sciences Journal | |
dc.subject | Enzyme activity | |
dc.subject | Metal complex | |
dc.subject | Proteinase Candida albicans | |
dc.subject | Zinc ion | |
dc.title | Interaction of secreted aspartic proteinase Candida albicans with ZnCl2: Complex formation and catalytic activity | |
dc.type | Article | |
dc.relation.ispartofseries-issue | 9 | |
dc.relation.ispartofseries-volume | 27 | |
dc.collection | Публикации сотрудников КФУ | |
dc.relation.startpage | 1225 | |
dc.source.id | SCOPUS18184952-2013-27-9-SID84890922868 |