The role of membrane proteins and phospholipids in the interaction of ribosomes with endoplasmic reticulum membranes.

Canadian Journal of Biochemistry
S JothyH Simpkins

Abstract

Hydrolysis of the membrane proteins and phospholipid headgroups of rat liver rough endoplasmic reticulum membranes showed that the ribosomal binding sites involve membrane proteins susceptible to low concentrations of trypsin, chymotrypsin, and papain. Three membrane proteins having molecular weights of 120 000, 93 000 and 36 000 are found to be altered by trypsin and chymotrypsin treatment. Also the polar headgroup of phosphatidylinositol appears to play a role in the binding process.

Citations

Feb 1, 1993·The Journal of Cell Biology·A J Savitz, D I Meyer
May 16, 1997·The Journal of Biological Chemistry·A J Savitz, D I Meyer
Oct 1, 1986·Journal of Biomolecular Structure & Dynamics·B Brosius, D Riesner
Nov 16, 1979·Biochimica Et Biophysica Acta·H C Hawkins, R B Freedman
Aug 9, 1977·Biochimica Et Biophysica Acta·G C Shore, J R Tata

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