J. Biochem, 1988, Vol. 104, No. 4 633-637
© 1988 Japanese Biochemical Society
research-article |
Isolation from Human Erythrocytes of a New Membrane Protein Which Inhibits the Formation of Complement Transmembrane Channels1
Department of Physiological Chemistry, School of Pharmaceutical Sciences, Showa University Shinagawa-ku, Tokyo 142
A protein which inhibited coplement channel formation was isolated from extracts of papain-digested human erythrocyte membranes using DEAE-Sephacel, Bio-Gel A0.5m column chromatographies, and preparative sodium dodecyl sulfate-polyacrylamide gel electrophoresis followed by transfer to nitrocellulose paper and elution with 2% NP-40 solution. The purified protein showed a molecular weight of 18 kDa, and efficiently inhibited hemolysis of EC5-7 cells with C8 and C9, but did not show any decay-accelerating activity to C5 convertase. Immunochemical analysis of native membranes after sodium dodecyl sulfate-polyacrylamide gel electrophoresis using the antibody against this protein gave a single band having the same mobility as this protein; papain did not eliminate a signifiant portion of this protein.
1This study was supported in part by a Grant-in-Aid for Scientific Research (No. 62580132) from the Ministry of Education, Science and Culture of Japan.
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