We have developed a procedure to isolate the ciliary membranes of Paramecium and have analysed the membrane proteins by electrophoresis on polyacrylamide gels containing either Triton X-100 or sodium dodecyl sulphate. The electrophoretic pattern on gels containing sodium dodecyl sulphate showed 12-15 minor bands of mol.wt. 25 000-150 000 and on major band of mol.wt. 200 000-300 000 that contained approximately three-quarters of the total membrane protein. 2. We present evidence that the major membrane protein is related to, but not identical with, the immobilization antigen (i-antigen), which is a large (250 000 mol.w.), soluble, surface protein of Paramecium. The similarity of the i-antigen and the major membrane protein was shown by immunodiffusion and by the electrophoretic mobilities in sodium dodecyl sulphate of these two proteins from Paramecium of serotypes A and B. The non-identity of these two proteins was shown by their different electrophoretic mobilities on Triton X-100 containing gels and their different solubilities. 3. We propose that the major membrane protein and the i-antigen have a precursor-product relationship.
Research Article|December 01 1975
Studies of the cell surface of Paramecium. Ciliary membrane proteins and immobilization antigens
H G Hansma;
Biochem J (1975) 152 (3): 523-528.
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H G Hansma, C Kung; Studies of the cell surface of Paramecium. Ciliary membrane proteins and immobilization antigens. Biochem J 1 December 1975; 152 (3): 523–528. doi: https://doi.org/10.1042/bj1520523
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