Oct, 1995
PURIFICATION OF PHOSPHOINOSITOL KINASE FROM SUSPENSION-CULTURED CELLS OF RICE (ORYZA-SATIVA L)
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
- ,
- ,
- Volume
- 59
- Number
- 10
- First page
- 1953
- Last page
- 1955
- Language
- English
- Publishing type
- Research paper (scientific journal)
- Publisher
- TAYLOR & FRANCIS LTD
Phosphoinositol kinase was purified from suspension-cultured rice (Oryza sativa L,) cells, The apparent molecular mass of the rice enzyme was estimated to be 58 kDa by SDS-PAGE and 234 kDa by Toyopearl HW-55S gel filtration, indicating that it is a tetrameric enzyme. The enzyme absolutely required Mg2+ for the activity, but Mn2+ and Ca2+ did not affect it. In addition, this kinase phosphorylated inositol monophosphate to phytate, Judging from these data, rice phosphoinositol kinase was concluded to be a different enzyme distinguished from the other plant phosphoinositol kinases.
- Link information
- ID information
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- ISSN : 0916-8451
- eISSN : 1347-6947
- Web of Science ID : WOS:A1995TC41200032