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

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.

authors

Hammelburger JW,Palfree RG,Sirlin S,Hämmerling U

doi

10.1016/s0006-291x(87)80275-9

subject

Has Abstract

pub_date

1987-11-13 00:00:00

pages

1304-11

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(87)80275-9

journal_volume

148

pub_type

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