Acylation in vivo of the contact site A glycoprotein and of other membrane proteins in Dictyostelium discoideum

FEBS Letters

Bauer, Gisela¹  Stadler, Joachim¹  Gerisch, Günther¹ 

[1] Max-Planck-Institut für Biochemie, D-8033 Martinsried bei München, FRG

关键词: Acylation;    Integral membrane glycoprotein;    Cell adhesion;    Dictyostelium discoideum;   

DOI  :  10.1016/0014-5793(84)81150-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Cells of Dictyostelium discoideum were incubated during the preaggregation phase with [³H] palmitic acid, and association of the fatty acid label with proteins was investigated by SDS-polyacrylamide gel electrophoresis and fluorography. Three proteins with apparent molecular masses of 44, 80 and 130kDa were preferentially labeled. The 80-kDa protein proved to be identical with an integral membrane glycoprotein called contact site A. The protein retained the ³H label after chloroform-methanol extraction and boiling in SDS-containing buffer, but not after mild hydroxylamine treatment, indicating an ester bond. After treatment of the protein with KOH the ³H label was recovered in free palmitic acid, as demonstrated by gas-liquid chromatography of the methyl ester.

【 授权许可】

Unknown