Linked Life Data

17385569

Source:http://linkedlifedata.com/resource/pubmed/id/17385569

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2007-3-27
pubmed:abstractText
Surfactants influence functions of proteins in cell signalling. Because molecular mechanisms of surfactants are poorly understood, the cationic surfactant effect on three metabolically important enzymes--L-glutamate dehydrogenase, L-lactate dehydrogenase, and L-malate dehydrogenase--were investigated at a physiologically relevant pH range (6.5-7.4). How a cationic, a non-ionic, and an anionic surfactant could differentially influence these enzymes, and how these surfactants could influence the interfacial mass transport of these enzymes across a polycarbonate membrane in a separation cell were also investigated. Provided the charge density was the same, cationic surfactants affected enzymatic activities similarly, regardless of their molecular masses. Hence, a cationic surfactant behaved similarly to a hydrophilic anionic surfactant; however, the cationic surfactant also enhanced enzymatic activity at pH 6.5 and a moderately high concentration (150 ppm). The hydrophilic surfactant enhanced enzymatic activity and the hydrophobic surfactant depressed enzymatic activity. Addition of 0.1 ppm of the hydrophilic anionic surfactant decreased the amount of enzyme permeation through the membrane, but 0.1 ppm of the non-ionic surfactant had no effect, whereas 0.1 ppm of the hydrophobic surfactant increased enzyme permeation. These results have physiological and signalling implications in nanobiotechnology.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0954-4119
pubmed:author
pubmed:issnType
Print
pubmed:volume
221
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
153-60
pubmed:dateRevised
2009-6-8
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Cationic surfactants and other factors that affect enzymatic activities and transport.
pubmed:affiliation
College of Engineering, Idaho State University, 833 S. 8th Ave, Pocatello, Idaho, 83209-8060, USA. leunsolo@isu.edu
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural