Proteins synthesized by rabbit reticulocyte membrane-bound ribosomes
- 30 April 1982
- journal article
- research article
- Published by Canadian Science Publishing in Canadian Journal of Biochemistry
- Vol. 60 (5) , 580-585
- https://doi.org/10.1139/o82-071
Abstract
Rabbit reticulocyte membrane-bound ribisomes liberated by deoxycholate treatment contain degraded forms of rRNA and mRNA. This degradation occurs after the liberation of the ribosomes from the membranes by the detergent because intact rRNA and mRNA can be extracted from washed membranes by phenol treatment. Increasing the ionic strength of the detergent buffer prevents this RNA degradation and allows the recovery of membrane-bound ribosomes capable of protein synthesis. Comparison of the proteins synthesized in vitro by the polyribosomes shows that the main protein produced by both free and membrane-bound ribosomes is globin. However, the 2 types of polyribosomes could be distinguished by the nonglobin proteins they produce.This publication has 3 references indexed in Scilit:
- An Efficient mRNA‐Dependent Translation System from Reticulocyte LysatesEuropean Journal of Biochemistry, 1976
- Properties of Membrane-bound Ribosomes in ReticulocytesJournal of Biological Chemistry, 1968
- The fractionation of high-molecular-weight ribonucleic acid by polyacrylamide-gel electrophoresisBiochemical Journal, 1967