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Distinct binding sites for Ins(1,4,5)P3 and Ins(1,3,4,5)P4 in bovine parathyroid glands

โœ Scribed by Peter Enyedi; Edward Brown; Gordon Williams


Book ID
115762410
Publisher
Elsevier Science
Year
1989
Tongue
English
Weight
459 KB
Volume
159
Category
Article
ISSN
0006-291X

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## Abstract PRIPโ€1 was isolated as a novel inositol 1,4,5โ€trisphosphate [Ins(1,4,5)P~3~] binding protein with a domain organization similar to phospholipase Cโ€ฮด1 (PLCโ€ฮด1) but lacking the enzymatic activity. Further studies revealed that the pleckstrin homology (PH) domain of PRIPโ€1 is the region re

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2-Fluoro-2-deoxy-lns(1,4,5)Ps (2) and 2,2-difluoro-Z-deoxy-Ins(l,4,5)P, (3) were synthesized from protected inositol precursors. The monofluoro compound with free 3,6-hydroxyl groups underwent slow defluorination at pH 1 13, as determined by laF-NMR, while the difluoro compound was inert. Cells can