Purification, properties, and N-terminal amino acid sequence of certain 50S ribosomal subunit proteins from the archaebacterium Halobacterium cutirubrum.

Autor: Matheson AT, Yaguchi M, Christensen P, Rollin CF, Hasnain S
Jazyk: angličtina
Zdroj: Canadian journal of biochemistry and cell biology = Revue canadienne de biochimie et biologie cellulaire [Can J Biochem Cell Biol] 1984 Jun; Vol. 62 (6), pp. 426-33.
DOI: 10.1139/o84-058
Abstrakt: Sixteen ribosomal proteins (r-proteins) from the 50S ribosomal subunit of the archaebacterium Halobacterium cutirubrum have been purified and their amino acid composition and partial N-terminal amino acid sequence have been 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 archaebacterial r-proteins and the equivalent proteins from the eubacterium Escherichia coli.
Databáze: MEDLINE