Escherichia coli phosphoenolpyruvate dependent phosphotransferase system. Complete purification of enzyme I by hydrophobic interaction chromatography

Biochemistry ◽  
1979 ◽  
Vol 18 (14) ◽  
pp. 2984-2989 ◽  
Author(s):  
G. T. Robillard ◽  
G. Dooijewaard ◽  
J. Lolkema
Keyword(s):  
Escherichia Coli ◽  
Hydrophobic Interaction ◽  
Hydrophobic Interaction Chromatography ◽  
Phosphotransferase System ◽  
Complete Purification ◽  
Enzyme I

A novel phosphoprotein dependent on the bacterial phosphoenolpyruvate–sugar phosphotransferase system

1983 ◽  
Vol 61 (2-3) ◽  
pp. 150-153 ◽  
Author(s):  
E. Bruce Waygood ◽  
Roshan L. Mattoo
Keyword(s):  
Escherichia Coli ◽  
Salmonella Typhimurium ◽  
Growth Conditions ◽  
Phosphotransferase System ◽  
Crude Extracts ◽  
Enzyme I ◽  
Novel Protein

A protein has been found by isoelectricfocusing and autoradiography in Escherichia coli and Salmonella typhimurium which was phosphorylated by enzyme I and an histidine-containing phosphocarrier protein (HPr) of the phosphoenolpyruvate–sugar phosphotransferase system (PTS). This protein was not factor IIIglc nor was it specifically induced by fructose. Its presence in soluble crude extracts was dependent upon growth conditions; however, the two bacteria had different patterns and amounts in respect to this novel protein. The protein was present in S. typhimurium SB2950 which has an extensive deletion through the pts operon, thus indicating that it must be coded for elsewhere on the genome.

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