Linked Life Data

7240229

Source:http://linkedlifedata.com/resource/pubmed/id/7240229

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
13
pubmed:dateCreated
1981-8-27
pubmed:abstractText
An alpha-mannosidase specific for the hydrolysis of alpha-1,2-mannosyl-mannose linkages has been solubilized and partially purified from rabbit liver microsomes. The enzyme is inhibited by EDTA and has optimal activity in the presence of calcium ions. The purified enzyme has a requirement for nonionic detergents or for specific phospholipids. At detergent concentrations appreciably below the critical micelle concentration, the enzyme is active in the presence of phosphatidylcholine or phosphatidylethanolamine but not with phosphatidylinositol, phosphatidylglycerol, or phosphatidic acid. At concentrations of phosphatidylcholine which provide optimal activity, the enzyme is strongly inhibited by phosphatidylinositol or phosphatidylglycerol. The substrate specificity of the alpha-mannosidase toward oligosaccharide substrates suggests that the enzyme may be involved in the processing of the oligosaccharide chains of mammalian glycoproteins.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
256
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6577-82
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
Purification and characterization of a phospholipid-dependent alpha-mannosidase from rabbit liver.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.