| Title : Removal of covalently bound inositol from Torpedo acetylcholinesterase and mammalian alkaline phosphatases by deamination with nitrous acid. Evidence for a common membrane-anchoring structure - Low_1987_Biochem.J_241_615 |
| Author(s) : Low MG , Futerman AH , Ackermann KE , Sherman WR , Silman I |
| Ref : Biochemical Journal , 241 :615 , 1987 |
|
Abstract :
Our earlier evidence suggested that both acetylcholinesterase and alkaline phosphatase are anchored to the cell surface via covalently-attached phosphatidylinositol [Low, Futerman, Ferguson & Silman (1986) Trends Biochem. Sci. 11, 212-215]. We now present chemical data, based upon a nitrous acid deamination reaction, showing that in both proteins the phosphatidylinositol moiety is attached through a glycosidic linkage to a sugar residue bearing a free amino group. |
| PubMedSearch : Low_1987_Biochem.J_241_615 |
| PubMedID: 3593210 |
Low MG, Futerman AH, Ackermann KE, Sherman WR, Silman I (1987)
Removal of covalently bound inositol from Torpedo acetylcholinesterase and mammalian alkaline phosphatases by deamination with nitrous acid. Evidence for a common membrane-anchoring structure
Biochemical Journal
241 :615
Low MG, Futerman AH, Ackermann KE, Sherman WR, Silman I (1987)
Biochemical Journal
241 :615