Purification, properties, and N-terminal amino acid sequence of certain 50S ribosomal subunit proteins from the archaebacterium Halobacterium cutirubrum
- 1 June 1984
- journal article
- research article
- Published by Canadian Science Publishing in Canadian Journal of Biochemistry and Cell Biology
- Vol. 62 (6) , 426-433
- https://doi.org/10.1139/o84-058
Abstract
Sixteen ribosomal proteins (r-proteins) from the 50S ribosomal subunit of the arachaebacterium H. cutirubrum were purified and their amino acid composition and partial N-terminal amino acid sequence were determined. These proteins as a group are much more acidic than the large subunit r-proteins from eubacteria or eukaryotes. Little sequence homology is evident between the 50S subunit arachaebacterial r-proteins and the equivalent proteins from the eubacterium Escherichia coli.This publication has 1 reference indexed in Scilit:
- The ribosomes of the extremely halophilic bacterium, Halobacterium cutirubrumJournal of Molecular Biology, 1964