Format

Send to

Choose Destination
Biochem Biophys Res Commun. 1987 Nov 13;148(3):1304-11.

Demonstration of phosphatidylinositol anchors on Ly-6 molecules by specific phospholipase C digestion and gel electrophoresis in octylglucoside.

Author information

1
Memorial Sloan-Kettering Cancer Center, New York, N.Y. 10021.

Abstract

Release by phosphatidylinositol-specific phospholipase 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.

PMID:
3318830
DOI:
10.1016/s0006-291x(87)80275-9
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center