Linked Life Data

2555532

Source:http://linkedlifedata.com/resource/pubmed/id/2555532

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1989-12-28
pubmed:abstractText
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 Km of 0.2 mM, and a Vmax of 150 nmoles/mg protein/hr. The enzyme had a specific requirement for Zn+2 with an optimum concentration at 0.25 mM. Maximum enzyme activity was at 50 degrees C and an Arrhenius plot showed a breakpoint at 40 degrees. 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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0360-4012
pubmed:author
pubmed:issnType
Print
pubmed:volume
24
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
231-40
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Glycerophosphorylcholine phosphocholine phosphodiesterase activity of rat brain myelin.
pubmed:affiliation
Department of Biochemistry, University of Manitoba, Winnipeg, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't