Abstract: |
Release by phosphatidylinositol-specific phospholiase C is frequently provided as evidence for membrane anchorage of a protein through phosphatidylinositol. Demonstration that the enzyme removes a lipophilic moiety from the protein is stronger evidence, and is presented here for members of the Ly-6 family of lymphocyte antigens: Ly-6A, C and E. Treatment of these molecules with the enzyme greatly increased their electrophoretic mobilities on polyacrylamide gels containing nonionic detergent. Furthermore, the mobilities of the digested, but not native Ly-6 molecules, were independent of detergent. This analytical method was applied to pure antigen, radiolabelled immunoprecipitate, or immunochemically detected Ly-6 antigens on blots. © 1987 Academic Press, Inc. |
Keywords: |
mouse; animal; mice; mice, inbred strains; enzyme immunoassay; immunoenzyme techniques; diagnostic agent; mouse strain; antigens, ly; ly antigen; polyacrylamide gel electrophoresis; electrophoresis, polyacrylamide gel; detergent; detergents; phosphatidylinositol; phosphatidylinositols; phospholipase c; article; support, u.s. gov't, p.h.s.; glucoside; octyl beta glucoside; octyl-beta-d-glucoside; glucosides
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