PURIFICATION AND PRIMARY STRUCTURE DETERMINATION OF THE N-TERMINAL BLOCKED PROTEIN, L11, FROM ESCHERICHIA-COLI RIBOSOMES
PURIFICATION AND PRIMARY STRUCTURE DETERMINATION OF THE N-TERMINAL BLOCKED PROTEIN, L11, FROM ESCHERICHIA-COLI RIBOSOMES
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DOI：
10.1111/j.1432-1033.1980.tb04995.x
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发表时间：
1980-01-01
期刊：
影响因子：
--
通讯作者：
WITTMANNLIEBOLD, B
中科院分区：
文献类型：
--
作者：
DOGNIN, MJ;WITTMANNLIEBOLD, B
Protein L11 was isolated from the 50-S subunit of E. coli ribosomes, using 2 salt extractions and 2 chromatographic separations of CM-cellulose. The unusual behavior of the protein when run on sodium dodecyl sulfate electrophoresis showed multiple bands. The complete primary structure of protein L11 is presented in detail. Its sequence was derived from peptides obtained by digesting the protein with trypsin, chymotrypsin, thermolysin, Staphylococcus aureus protease and, after modification, with trypsin. Chemical cleavage was performed with cyanogen bromide. Sequencing of the various peptides was achieved by manual micro-dansyl-Edman degradations and automatic methods. The N-terminal residue of the protein is blocked and was not degradable in the liquid-phase sequenator by the Edman method. It was idetnfied by a combination of enzymatic cleavage and mass spectrometry. Protein L11 contains 3 methylated amino acid residues, a N.alpha.-trimethylalanine and 2 residues of N.epsilon.-trimethyllysine. Their behavior and influence in the sequence elucidation are described. The protein contains 141 amino acid residues and has a MW of 14,874. Secondary structure predictions of the protein are given, and its sequence is compared with those of other E. coli ribosomal proteins.
