Isoelectric points and molecular weights of salt-extractable ribosomal proteins
- 1 December 1976
- journal article
- research article
- Published by Canadian Science Publishing in Canadian Journal of Biochemistry
- Vol. 54 (12) , 1029-1033
- https://doi.org/10.1139/o76-150
Abstract
Rat liver ribosomes prepared in low salt buffer contain basic and acidic proteins not found on ribosomes washed in high salt buffer. Proteins extracted from liver ribosomes by 500 mM KCl were characterized by acid urea-polyacrylamide gel electrophoresis, sodium dodecyl sulfate-polyacrylamide gel electrophoresis and gel isoelectric focusing. The salt-solubilized proteins contain 12 polypeptides with a MW over 67,000, several polypeptides with MW less than 67,000 and 3 polypeptides whose MW exceeded 130,000. Ten to 12 of the proteins were basic, and about 24 acidic proteins were partially or wholly extracted from the ribosomes. Four of the acidic proteins have isoelectric points less than 4.5.This publication has 3 references indexed in Scilit:
- Ultracentrifugal studies on the dissociation of hepatic ribosomesJournal of Molecular Biology, 1965
- THE CHROMOSOMAL SITE SPECIFYING A RIBOSOMAL PROTEIN IN ESCHERICHIA COLIProceedings of the National Academy of Sciences, 1964
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951