Linked Life Data

2818611

Source:http://linkedlifedata.com/resource/pubmed/id/2818611

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1989-12-11
pubmed:abstractText
Bovine liver dihydrofolate reductase has been solubilized in reverse micelles of cationic surfactant cetyltrimethylammonium bromide (CTAB) in isooctane-chloroform (1:1,V/V) mixture. Variation of waterpool (WO), pH and surfactant concentration showed that the enzyme activity was regulated by these parameters and was higher than the activity found in aqueous buffer (defined as superactivity); the maximum being at WO 13.3, pH 7.0 and CTAB concentration 75 mM. The Michaelis constants, Km for the substrate FAH2 and NADPH were found to be greater than those determined in water. Since reverse micelles have some features similar to those of biomembranes, display of super activity by dihydrofolate reductase indicates that enzymes in vivo may possess higher activity than actually observed in vitro studies in aqueous solutions.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0158-5231
pubmed:author
pubmed:issnType
Print
pubmed:volume
19
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
547-52
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
The phenomenon of super activity in dihydrofolate reductase entrapped inside reverse micelles in apolar solvents.
pubmed:affiliation
Department of Chemistry, Indian Institute of Technology, Kanpur.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't