Linked Life Data

8305458

Source:http://linkedlifedata.com/resource/pubmed/id/8305458

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1994-3-15
pubmed:abstractText
The interaction of lipase from Candida cylindracea (CCL) with positively charged polymerizable surfactant vesicles was studied by the use of steady-state fluorescence techniques. The phase transition of vesicles composed of nonpolymerized and polymerized N-allylbis[2-(hexadecanoyloxy)ethyl]methylammonium bromide (ABHEMA Br) was determined in the absence of lipase, by measuring the change in fluorescence anisotropy of the membrane probe 1,6-diphenyl-1,3,5-hexatriene (DPH). The phase transition temperature for nonpolymerized vesicles is 49 degrees C and for the polymerized analogues 45 degrees C. Fluorescence anisotropy and resonance energy transfer measurements were used to illustrate the incorporation of the lipase in the vesicle membrane. These studies demonstrated that CCL is incorporated into the hydrophobic bilayer of the vesicle. By using an interfacial membrane probe 1-[4-(trimethylammonium)phenyl]-6-phenyl-1,3,5-hexatriene p-toluene sulphonate, TMA-DPH) and an internal membrane probe (DPH), it could be determined that the enzyme is incorporated more efficiently into nonpolymerized vesicles, and that the penetration of the enzyme into the bilayer is less deep in the case of the polymerized vesicles.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
3
pubmed:volume
1189
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
45-51
pubmed:dateRevised
2005-11-17
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Steady-state fluorescence studies on lipase-vesicle interactions.
pubmed:affiliation
Dept. of Organic Chemistry, Wageningen Agricultural University, The Netherlands.
pubmed:publicationType
Journal Article