Lahiri Majumder, A. N. ; Mandal, N. C. ; Biswas, B. B. (1972) Phosphoinositol kinase from germinating mung bean seeds Phytochemistry, 11 (2). pp. 503-508. ISSN 0031-9422
Full text not available from this repository.
Official URL: http://linkinghub.elsevier.com/retrieve/pii/003194...
Related URL: http://dx.doi.org/10.1016/0031-9422(72)80004-9
Abstract
Phosphoinositol kinase (adenosine triphosphate-inositolmonophosphate phospho-tranferase) has been isolated from cotyledons; about 300-fold purification has been achieved, with a recovery of 11%. The enzyme has a pH optimum at 7 ·4. It can mediate phosphorylation of lower inositol phosphates to their corresponding higher homologues, ATP being the phosphate donor. ATP can be replaced partially by UTP and PEP. The enzyme requires divalent cations for the reaction. Mn2+ has been found to be twice as effective as Mg2+, Ca2+ being inhibitory. Phosphoinositol kinase has been found to be different from inositol kinase.
| Item Type: | Article |
|---|---|
| Source: | Copyright of this article belongs to Phytochemical Society of Europe. |
| ID Code: | 3533 |
| Deposited On: | 12 Oct 2010 04:18 |
| Last Modified: | 18 Jul 2012 03:23 |
Repository Staff Only: item control page
