Proteins of the Thermus thermophilus ribosome. Purification of proteins from the large ribosomal subunit.
Special procedures have been developed to isolate and purify 26 of the 30 individual proteins of the large ribosomal subunit from Thermus thermophilus. Sixteen of them have been purified under non-denaturing conditions to be used for crystallization and further structural studies. These proteins have been characterized by their amino acid content, molecular mass, UV-spectrum and extinction coefficient. An additional 10 proteins have been purified by reverse phase chromatography. Thirteen proteins have been identified by homological E coli proteins.
Institute of Protein Research, Russian Academy of Sciences, Puschchino, Moscow region.
S E
SE
Sedelnikova
O S
OS
Shikaeva
N K
NK
Avlijakulov
T A
TA
Muranova
L F
LF
Markova
I A
IA
Kashparov
M B
MB
Garber
D000595:Amino Acid Sequence; D002852:Chromatography, Ion Exchange; D015180:Electrophoresis, Gel, Two-Dimensional; D008969:Molecular Sequence Data; D008970:Molecular Weight; D012269:Ribosomal Proteins / Q000302:isolation & purification*; D012270:Ribosomes / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D013056:Spectrophotometry, Ultraviolet; D016963:Thermus thermophilus / Q000378:metabolism*
D012269:Ribosomal Proteins