Abstract
AbstractThe 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.
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