Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1984-1-7
pubmed:abstractText
A partially purified microsomal alpha-1,2-mannosidase from rabbit liver binds to vesicles that contain anionic phospholipids. The affinity of the enzyme for the phospholipid vesicles is dependent upon the negative charge density of the vesicles rather than the concentration of the anionic phospholipid or the phospholipid specificity. A phosphatidylinositol/phosphatidylcholine ratio of 1:3 is sufficient to bind all of the enzyme. The association of enzyme with anionic phospholipids involves ionic interactions and can be readily reversed by high ionic strength or changes in pH. The alpha-mannosidase is inhibited when bound to the anionic phospholipid vesicles, but the enzyme can be reactivated when released by NaCl or CaCl2. When bound to anionic phospholipid vesicles, the enzyme was also found to undergo a slow inactivation process that was time and temperature dependent and could not be reversed by the addition of CaCl2.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
136
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
577-82
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
Interaction of alpha-1,2-mannosidase with anionic phospholipids.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't