Linked Life Data

7284310

Source:http://linkedlifedata.com/resource/pubmed/id/7284310

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
14
pubmed:dateCreated
1981-12-21
pubmed:abstractText
Porcine pancreatic phospholipase A2 interacts with micelles of the substrate analogue n-octadecylphosphocholine to form a specific complex over considerably wide concentration ranges of both lipid and protein. UV absorption difference spectroscopy measurements indicate that the ratio of lipid to protein molecules in the complex is approximately 50. This number is confirmed by using other techniques to study the composition of the complex, namely, ultracentrifugation experiments and light scattering. The latter techniques furthermore demonstrate that the lipid--protein complex consists of 100 lipid and 2 enzyme molecules. Thus, the number of lipid molecules in the free micelle (200) is halved when the complex with phospholipase is being formed. The consequences of the results are discussed in relation to a theoretical model of the lipid--protein interaction.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
7
pubmed:volume
20
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4068-73
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
Physicochemical studies on the interaction of pancreatic phospholipase A2 with a micellar substrate analogue.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't