Linked Life Data

1213878

Source:http://linkedlifedata.com/resource/pubmed/id/1213878

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1976-4-27
pubmed:abstractText
Mitochondrial membranes reconstituted from lipid-depleted mitochondria and aqueous phospholipid dispersions still have the phospholipid negative charges available for ionic interaction with the basic protein, lysozyme. The stoichiometry of the binding is of about 6 nmoles of lysozyme per 100 nmoles of phospholipid in membranes reconstituted with Asolectin, and of 10 nmoles of phospholipid phosphorus in membranes reconstituted with cardiolipin. Unextracted submitochondrial particles ETP also bind lysozyme (about 3 nmoles per 100 nmoles of phospholipid). These observations indicate that the phospholipid anionic groups are not completely shielded by the mitochondrial proteins, which might occupy areas between the nonpolar groups of the lipid molecules.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0021-2938
pubmed:author
pubmed:issnType
Print
pubmed:volume
24
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
269-77
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:articleTitle
Fromation and stoichiometry of a lysozyme-phospholipid-mitochondrial protein ternary complex.
pubmed:publicationType
Journal Article