Linked Life Data

3127263

Source:http://linkedlifedata.com/resource/pubmed/id/3127263

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1988-5-12
pubmed:abstractText
The immobilization of drug-metabolizing enzymes onto polymeric supports offers several advantages over use of conventional microsomal or soluble enzyme preparations. These include increased storage stability, facilitated separation of products from the incubation mixture, the ability to recover and reuse the enzyme catalyst, and in many cases, stabilization of the tertiary structure of membrane-bound enzymes. Attachment of the protein to the solid support may be accomplished by adsorption, covalent bonding, or entrapment techniques. This methodology has been successfully utilized for studies with such enzymes as cytochrome P-450, UDP-glucuronyltransferases, glutathione S-transferases, S-methyltransferases, and N-acetyltransferases. Although often employed for the synthesis of xenobiotic metabolites, immobilized enzymes have been used for mechanistic and relative reactivity studies, limited kinetic studies, and extracorporeal detoxification. Co-immobilization of multiple drug-metabolizing enzyme systems has made possible the sequential formation of metabolites arising from oxidation followed by conjugation. Immobilized enzymes may also be used in the prediction of species-dependent metabolic pathways. The potential for large-scale synthesis of drug metabolites using this methodology has been explored.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0892-6638
pubmed:author
pubmed:issnType
Print
pubmed:volume
2
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2235-40
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Use of immobilized enzymes in drug metabolism studies.
pubmed:affiliation
Department of Pharmacology and Molecular Sciences, Johns Hopkins School of Medicine, Baltimore, Maryland 21205.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Review