Linked Life Data

14512636

Source:http://linkedlifedata.com/resource/pubmed/id/14512636

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2003-9-26
pubmed:abstractText
Glucose oxidase (GOD) is often used in immobilized forms for determination of glucose. To examine the possibility of its adsorption by hydrophobic interactions, palmityl-substituted Sepharose 4B (Sepharoselipid) was employed as an adsorptive matrix. Various conditions were used in tests to improve the limited immobilization of the enzyme observed under normal (native) conditions, including use of high concentrations of denaturing agents. Of the denaturants used, only the cationic detergent dodecyl trimethyl ammonium bromide was effective in denaturing the protein and exposing its hydrophobic sites for interaction with alkyl residues on the support. This, followed by the process of renaturation, provided catalytically active immobilized preparations. The apoenzyme, prepared by treatment of the holoenzyme with acidified (NH4)2SO4 or thermal denaturation, was totally immobilized on the support. Furthermore, it was shown that either flavin adenine dinucleotide (FAD) or the alkyl residues, not both, may interact with the nucleotide site at any given time. Results are discussed in terms of high rigidity of GOD molecule and limited exposure of hydrophobic sites in its native structure. The observations are in accord with suggestions in the literature that the FAD pocket is a very narrow channel of hydrophobic properties, adapted to accept its natural coenzyme.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0273-2289
pubmed:author
pubmed:issnType
Print
pubmed:volume
110
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
165-74
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Interaction of glucose oxidase with alkyl-substituted Sepharose 4B.
pubmed:affiliation
Institute of Biochemistry and Biophysics, University of Tehran, PO Box 13145-1384, Tehran, Iran.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't