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pubmed-article:10874982rdf:typepubmed:Citationlld:pubmed
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pubmed-article:10874982pubmed:abstractTextGlucose 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.lld:pubmed
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pubmed-article:10874982pubmed:statusMEDLINElld:pubmed
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pubmed-article:10874982pubmed:authorpubmed-author:RigoAAlld:pubmed
pubmed-article:10874982pubmed:authorpubmed-author:VianelloFFlld:pubmed
pubmed-article:10874982pubmed:authorpubmed-author:ZennariRRlld:pubmed
pubmed-article:10874982pubmed:authorpubmed-author:Di PaoloM LMLlld:pubmed
pubmed-article:10874982pubmed:authorpubmed-author:BortoluzziSSlld:pubmed
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pubmed-article:10874982pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:10874982pubmed:articleTitleCharacterization of thin layers of glucose oxidase.lld:pubmed
pubmed-article:10874982pubmed:affiliationDepartment of Biological Chemistry, University of Padova.lld:pubmed
pubmed-article:10874982pubmed:publicationTypeJournal Articlelld:pubmed