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dc.contributor.author | Sharipova M. | |
dc.contributor.author | Balaban N. | |
dc.contributor.author | Nekhotyaeva N. | |
dc.contributor.author | Mardanova A. | |
dc.contributor.author | Dementiev A. | |
dc.contributor.author | Leshchinskaya I. | |
dc.date.accessioned | 2018-09-17T21:01:40Z | |
dc.date.available | 2018-09-17T21:01:40Z | |
dc.date.issued | 1996 | |
dc.identifier.issn | 1039-9712 | |
dc.identifier.uri | https://dspace.kpfu.ru/xmlui/handle/net/134416 | |
dc.description.abstract | A new alkaline phosphatase was obtained as homogeneous preparation from culture filtrate of the spore-forming Bacillus intermedius. B. intermedius phosphatase was shown to be monomer with molecular weight of 47 kDa. The enzyme possesses phosphomonoesterase and phosphodiesterase activities and exhibits a broad specificity towards a wide variety of substrates. The purified phosphatase had an optimum temperature of 50°C, optimum pH of 9.5 and was stable until 60°C at pH 8-10. The effect of divalent metal ions and thiol reagents on catalytic activity of the enzyme was studied. | |
dc.relation.ispartofseries | Biochemistry and Molecular Biology International | |
dc.subject | Alkaline phosphatase | |
dc.subject | Inhibition | |
dc.subject | Purification | |
dc.subject | Substrate specificity | |
dc.title | A novel Bacillus intermedius extracellular alkaline phosphatase: Isolation, physico-chemical and catalytic characteristics | |
dc.type | Article | |
dc.relation.ispartofseries-issue | 4 | |
dc.relation.ispartofseries-volume | 38 | |
dc.collection | Публикации сотрудников КФУ | |
dc.relation.startpage | 753 | |
dc.source.id | SCOPUS10399712-1996-38-4-SID0029775085 |