Analysis of Escherichia coli Ribosomal Proteins by an Improved Two Dimensional Gel Electrophoresis. II. Characterization of Fonr New Proteins

1986 ◽  
Vol 100 (6) ◽  
pp. 1595-1605 ◽  
Author(s):  
Akira WADA
Keyword(s):  
Escherichia Coli ◽  
Gel Electrophoresis ◽  
Ribosomal Proteins ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis

Identification and quantitation of elongation factor EF-P in Escherichia coli cell-free extracts

1980 ◽  
Vol 58 (11) ◽  
pp. 1312-1314 ◽  
Author(s):  
Gynheung An ◽  
Bernard R. Glick ◽  
James D. Friesen ◽  
M. Clelia Ganoza
Keyword(s):  
Escherichia Coli ◽  
Molecular Weight ◽  
Protein Synthesis ◽  
Gel Electrophoresis ◽  
Ribosomal Proteins ◽  
Elongation Factor ◽  
Peptide Bond ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis

EF-P, an elongation factor that stimulates peptide bond synthesis in vitro with some aminoacyl-tRNAs, has been identified by two-dimensional gel electrophoresis and the cellular content at three points in the growth curve has been measured. The molecular weight of EF-P is estimated to be 21 000. EF-P is a slightly acidic protein whose isoelectric point is close to RNA polymerase subunit α. The amount of EF-P present in Escherichia coli is about [Formula: see text]that of EF-G and the level is independent of the stage of cell growth; there is about one EF-P per 10 ribosomes. It is also shown that a highly purified preparation of EF-P is free of all known protein synthesis factors and ribosomal proteins.

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