Phosphatidylinositol-attached 5'-nucleotidase from synaptic plasma membrane of rat brain.
Synaptic plasma membranes (SPM) of rat brain contained a 5'-nucleotidase that was specifically released by Bacillus thuringiensis phosphatidylinositol-specific phospholipase C (PIPLC). About 30% of the enzyme was readily released and the remainder was less susceptible. Purified 5'-nucleotidase was treated with PIPLC and the resultant enzyme was almost totally partitioned into the detergent-poor phase following phase-separation in Triton X-114 indicating that PIPLC converted the enzyme from an amphipathic to a hydrophilic form. The results suggest that 5'-nucleotidase is anchored into SPM by a covalently attached phosphatidylinositol moiety.
Lai
K M
KM
Department of Biochemistry, University of Hong Kong.
Wong
P C
PC
D015720:5'-Nucleotidase / Q000378:metabolism*; D000818:Animals; D002540:Cerebral Cortex / Q000378:metabolism; D066298:In Vitro Techniques; D043265:Phosphatidylinositol Diacylglycerol-Lyase; D010716:Phosphatidylinositols / Q000378:metabolism*; D054801:Phosphoinositide Phospholipase C; D010727:Phosphoric Diester Hydrolases / Q000494:pharmacology; D051381:Rats; D013570:Synaptic Membranes / Q000187:drug effects / Q000378:metabolism*
D010716:Phosphatidylinositols; D015720:5'-Nucleotidase; D010727:Phosphoric Diester Hydrolases; D054801:Phosphoinositide Phospholipase C; D043265:Phosphatidylinositol Diacylglycerol-Lyase