๐”– Bobbio Scriptorium
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Glycerophosphorylcholine phosphocholine phosphodiesterase activity of rat brain myelin

โœ Scribed by Dr. J. N. Kanfer; D. G. McCartney

Publisher
John Wiley and Sons
Year
1989
Tongue
English
Weight
705 KB
Volume
24
Category
Article
ISSN
0360-4012

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โœฆ Synopsis

Myelin isolated from rat brain possessed the ability to release phosphorylcholine from glycerophosphorylcholine, and this activity was enriched 3.2-fold over that of the original homogenate. This glycerophosphorylcholine phosphocholine phosphodiesterase activity had a pH optimum at 9.5, had a K, of 0.2 mM, and a V,,, of 150 nmoledmg proteidhr. The enzyme had a specific requirement for Zn+* with an optimum concentration at 0.25 mM. Maximum enzyme activity was at 50ยฐC and an Arrhenius plot showed a breakpoint at 40". p-Nitrophenylphosphorylcholine was also hydrolyzed by purified myelin and was a competitive inhibitor of glycerophosphorylcholine phosphocholine phosphodiesterase activity with a Ki of 0.075 mM. Glycerolphosphorylethanolamine was hydrolyzed only 5% compared with GPC, but it was not an inhibitor.

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