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Electrochemical Charge and Protein Adsorption

Published online by Cambridge University Press:  26 February 2011

Herbert J. Mueller
Herbert J. Mueller*
Affiliation:
Council on Dental Materials, Instruments and Equipment Division of Scientific Affairs, American Dental Association 211 East Chicago Avenue, Chicago, Illinois 60611
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Abstract

The amount of albumin adsorbed to three dental crown and bridge alloys (high- and low-gold content and silver-palladium), platinum, silver, and stainless steel was quantitated for the as-immersed conditions as well as with anodic and cathodic charge transfers in artifical saliva at a pH = 6.8. A methanolchloroform technique was utilized prior to protein assay which precipitated protein by phase separation. Amido black staining of protein on nitrocellulose filter paper was evaluated for optical density and compared to a standard curve of known quantities of protein. Cathodic charges decreased the quantity of adsorbed protein while anodic charges both increased and decreased adsorbed protein depending upon metal or alloy. Quantities adsorbed ranged from 0.5 to 8 μg/cm2. Interaction of positive oxidized species with the excess negative charges of the albumin molecules is thought to have increased protein adsorption. Formation of corrosion products with inorganic conponents is thought to have masked positive charges from protein thereby decreasing adsorption.

Type
Research Article
Information
MRS Online Proceedings Library (OPL) , Volume 110: Symposium M – Biomedical Materials and Devices , 1987 , 605
Copyright
Copyright © Materials Research Society 1988

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