Source:http://linkedlifedata.com/resource/pubmed/id/10874982
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
7-8
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pubmed:dateCreated |
2000-7-19
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pubmed:abstractText |
Glucose Oxidase (GOD) has been covalently bound to functionalized glass cover slips. The surface density of immobilized GOD molecules was measured by a method based on the amperometric determination of Flavin Adenine Dinucleotide (FAD). Atomic Force Microscopy (AFM) images, obtained in aqueous solution for the covalently bound enzyme, show a monomolecular layer of the enzyme on a functionalized glass surface. The catalytic constants were measured for the immobilized GOD and compared with those of the free enzyme.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:issn |
0037-8771
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
74
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
61-6
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading | |
pubmed:articleTitle |
Characterization of thin layers of glucose oxidase.
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pubmed:affiliation |
Department of Biological Chemistry, University of Padova.
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pubmed:publicationType |
Journal Article
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