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dc.contributor.authorSuci, Peter A.
dc.contributor.authorGeesey, Gill G.
dc.date.accessioned2018-01-17T23:32:53Z
dc.date.available2018-01-17T23:32:53Z
dc.date.issued2000-10
dc.identifier.citationSuci, P.A. and G.G. Geesey, "Influence of Sodium Periodate and Tyrosinase on Binding of Alginate to Adlayers of Mytilus edulis Foot Protein 1,"" Journal of Colloid and Interface Science, 230:3 (2000).en_US
dc.identifier.issn0021-9797
dc.identifier.urihttps://scholarworks.montana.edu/xmlui/handle/1/14146
dc.description.abstractMytilus edulis foot protein 1 (Mefp-1) is the most well-characterized component of this sea mussel's adhesive plaque. The plaque is a condensed, heterogeneous mixture consisting of a large proportion of cross-linked biopolymers that bonds the mussel to a chosen mooring. Mefp-1 is densely populated with lysine and L-3,4-dihyroxyphenylalanine (L-dopa) residues incorporated into a repeating amino acid sequence motif. It has been proposed that one plaque cross-linking reaction is the nucleophilic addition of the ϵ-amino groups of the lysine residues into the oxidized catechol (o-diphenol) functionality (quinone) of the L-dopa residues. In order to determine if this reaction occurs in adlayers of Mefp-1, a previously developed assay for ϵ-amino groups was applied. Adlayers of Mefp-1 were exposed to an oxidant, either the enzyme, mushroom tyrosinase, or sodium periodate. Binding of alginate to adlayers was used to probe for accessibility of ϵ-amino groups. It was found that lysine residues lose the ability to bind alginate after exposure to sodium periodate, but that this loss is not clearly due to a reaction with L-dopa residues. There is a slight decrease of binding of alginate to adlayers of Mefp-1 exposed to either active or thermally deactivated mushroom tyrosinase, probably due to the obstruction of binding sites by bound enzyme. Adsorption kinetics of mushroom tyrosinase onto adlayers of Mefp-1 for active and thermally inactivated enzyme were nearly identical. Attenuated total reflection Fourier transform infrared spectroscopy was used to characterize these interactions at a germanium (Ge) interface.en_US
dc.titleInfluence of sodium periodate and tyrosinase on binding of alginate to adlayers of mytilus edulis foot protein 1en_US
dc.typeArticleen_US
mus.citation.extentfirstpage340en_US
mus.citation.extentlastpage348en_US
mus.citation.issue2en_US
mus.citation.journaltitleJournal of Colloid and Interface Scienceen_US
mus.citation.volume230en_US
mus.identifier.categoryEngineering & Computer Scienceen_US
mus.identifier.doi10.1006/jcis.2000.7120en_US
mus.relation.collegeCollege of Engineeringen_US
mus.relation.departmentCenter for Biofilm Engineering.en_US
mus.relation.departmentChemical & Biological Engineering.en_US
mus.relation.departmentChemical Engineering.en_US
mus.relation.universityMontana State University - Bozemanen_US
mus.relation.researchgroupCenter for Biofilm Engineering.en_US
mus.data.thumbpage4en_US


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