THE ISOLATION AND COMPLETE AMINO-ACID-SEQUENCE OF THE RIBOSOMAL-PROTEIN L36 FROM THERMUS-THERMOPHILUS AND ITS ZINC-BINDING MOTIVE

Authors
BOYSEN RI LORENZ S KIM JS SCHRODER WFKJ ERDMANN VA
Citation
Ri. Boysen et al., THE ISOLATION AND COMPLETE AMINO-ACID-SEQUENCE OF THE RIBOSOMAL-PROTEIN L36 FROM THERMUS-THERMOPHILUS AND ITS ZINC-BINDING MOTIVE, Endocytobiosis and cell research, 11(1), 1995, pp. 41-57
Citations number
75
Categorie Soggetti
Cell Biology",Biology
Journal title
Endocytobiosis and cell research → ACNP
ISSN journal
02561514
Volume
11
Issue
1
Year of publication
1995
Pages
41 - 57
Database
ISI
SICI code
0256-1514(1995)11:1<41:TIACAO>2.0.ZU;2-W
Abstract
The ribosomal protein L36 of the thermophilic bacterium Thermus thermo philus was separated by a newly developed analytical method of Reverse d Phase Chromatography and subsequently gas phase sequenced without cl eavage in one single step. The complete sequence of the 37 amino acids , containing a zinc-binding motive, is presented. Furthermore, the N-t erminal sequences of L5, L9, L18, L24, L32, L33 and L35 from Thermus t hermophilus are shown.