Sulfhydryl and disulfide groups of platelet membranes. II. Determination of disulfide groups

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Abstract

Two methods are described and evaluated for the quantitative determination of disulfide (SS) bonds of platelet membrane proteins. In one method cleavage of SS bonds by sulfite was followed by reaction of the resultant monothiols with 203Hg-labeled p-chloromercuribenzoate. The mercurial adducts of the membrane proteins were measured by a nitrocellulose-filter assay. The other method was based on the reduction of disulfide bonds by dithiothreitol and the spectrophotometric determination of te sulfhydryl groups with dithiobisnitrobenzoic acid. Several variables of these assay systems including pH, urea and sulfite concentration were examined. Both methods yielded a similar number of SS groups in membrane proteins.

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