The Effect of Diamide (Azodicarboxylic Acid-bis-Dimethylamide) on Sulfhydryl Group Content, Proteins, and the Location of Phosphatidylethanolamine in Human Blood Platelets

Treatment of human blood platelets with the thiol-oxidizing agent, diamide, causes rapid oxidation of glutathione and alterations in aggregation and release reaction. Moreover, cross-linking of proteins was observed. Three high molecular weight bands of 200 - 240 X 10(3) daltons and a band of 66 X 10(3) daltons were involved in this process. After reduction with dithiotreitol the normal pattern was received. In contrast to the erythrocyte, the cross-linking of platelet proteins was not accompanied by a reorientation of phosphatidylethanolamine in the membrane. Also a considerably smaller effect of diamide on platelet protein sulfhydryl group content was measured.