Papers

Oct, 1995

PURIFICATION OF PHOSPHOINOSITOL KINASE FROM SUSPENSION-CULTURED CELLS OF RICE (ORYZA-SATIVA L)

BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
  • K YOTSUSHIMA
  • ,
  • T MITSUI
  • ,
  • T HAYAKAWA

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.

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Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:A1995TC41200032&DestApp=WOS_CPL
ID information
  • ISSN : 0916-8451
  • eISSN : 1347-6947
  • Web of Science ID : WOS:A1995TC41200032

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