Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
23
pubmed:dateCreated
1998-6-30
pubmed:abstractText
Colipase is a cofactor protein which forms a 1:1 complex with pancreatic lipase. This facilitates lipase adsorption to phosphatidylcholine-rich interfaces, presumably as a consequence of the higher affinity of colipase for such interfaces. According to this model, the presence of colipase in an interface should be sufficient to enable lipase adsorption from the aqueous phase. To test this hypothesis, mixed monolayers of colipase, phosphatidylcholine, and fatty acid at the argon-buffer interface were exposed to lipase injected into the stirred aqueous subphase. Spread colipase remained associated with the lipid monolayer in a surface pressure- and lipid composition-dependent manner. For example, with diacylphosphatidylcholine alone, colipase remained in the lipid monolayer at surface pressures </=20 mN/m, but with pure fatty acid this was increased to approximately 40 mN/m. Contrary to the existing paradigm, the presence of colipase in a lipid monolayer was not sufficient to enable the adsorption of lipase to the interface. Fatty acid was also required, and its ability to enhance lipase adsorption over that observed in the absence of colipase was dependent on the fatty acid and colipase mole fractions. These results support the hypothesis that colipase concentrates fatty acids laterally at its periphery and suggest that, together with lipase-colipase interaction, the fatty acid-rich nano-domain surrounding colipase facilitates lipase adsorption in the 'flap-opened' conformation.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
9
pubmed:volume
37
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
8369-77
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
How colipase-fatty acid interactions mediate adsorption of pancreatic lipase to interfaces.
pubmed:affiliation
The Hormel Institute, University of Minnesota, Austin 55912, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't