Abstract
The membrane protein of rat erythrocytes, solubilized by 1 % sodium dodecyl sulfate, was analyzed by polyacrylamide gel electrophoresis. Six major protein bands (Coomassie brilliant blue positive, I-VI, molecular weight: 200, 000, 170, 000, 105, 000, 96, 000, 80, 000 and 54, 000) or three glycoprotein bands (PAS positive, 1-3, molecular weight: 108, 000, 96, 000 and 54, 000) were detected in the membrane produced by hypotonic hemolysis. Several additional protein bands (between 90, 000-40, 000 molecular weight) were detected in the membrane produced by mercuric chloride, methylmercuric chloride and N-ethylmaleimide hemolysis. A smaller number of bands (90, 000-40, 000 molecular weight) were detected in the membrane produced by p-chloromercuribenzoic acid hemolysis than the membrane hemolyzed by other mercurials. However, those additional bands did not appear when membranes were produced by hypotonic hemolysis then treated with mercurials. A band under band IV appeared when p-chloromercuribenzoic acid was used for the treatment. The profile of PAS positive bands of membrane produced by mercurial hemolysis was similar to that of membrane produced by hypotonic hemolysis. The degree of free sulfhydryl groups in membrane treated with mercurials was not closely related to the induction of hemolysis.
