Specificity of the purified inositol (1,3,4,5) tetrakisphosphate‐binding protein from porcine platelets

FEBS Letters

Chang, Young-Tae¹  Chung, Sung-Kee¹  Irvine, Robin F.³  Cullen, Peter J.²  Dawson, Alan P.² 

[1] Department of Chemistry, Pohang University of Science and Technology, Pohang 790-784, South Korea;School of Biological Sciences, University of East Anglia, Norwich, Norfolk, NR4 7TJ, UK;Inositide Laboratory, The Babraham Institute, Babraham, Cambridge, CB2 4AT, UK

关键词: Inositol;    Inositol tetrakisphosphate;    Binding protein;    Platelet;    Procine;    Receptor;    All inositol phosphate isomers are given in D-numbering unless otherwise stated;   

DOI  :  10.1016/0014-5793(94)01435-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The specificity of the inositol 1,3,4,5-tetrakisphosphate binding protein purified from porcine platelets [Cullen et al. (1995) Biochem. J. 305, 139–143] was examined using all the isomers of myo-inositol tetrakisphosphate. From the relative potencies of these compounds it appears that phosphorylation of the 1, 3 and 5 positions is essential for high affinity binding, that there is some tolerance of phosphorylation of the 6-hydroxyl, but none of a phosphate in the 2-position, and that phosphorylation of the 4-hydroxyl has very little influence. The binding of Ins(1,3,4,5)P₄ was not appreciably altered by physiological Mg²⁺ concentrations, and the pH dependence of binding under physiological conditions showed a decline from pH 5.5 to pH 9.0.

【 授权许可】

Unknown