Abstract
A rapid, high-yield procedure has been developed for the purification of HPr from the Escherichia coli phosphoenolpyruvate dependent phosphotransferase system. During this procedure, the protein copurifies with a 2500-dalton homopolysaccharide which we have identified as alpha 1-6 glucan. The results of steady-state kinetic measurements of the phosphotransferase activity demonstrate that the polysaccharide works as an activator of the phosphotransferase system probably at the level of the HPr:P-E1 complex or the P-HPr:E11 complex.
MeSH terms
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Bacterial Proteins / isolation & purification*
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Carbohydrates / analysis
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Chemical Phenomena
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Chemistry
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Escherichia coli / enzymology*
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Glucans / isolation & purification*
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Magnetic Resonance Spectroscopy
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Models, Biological
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Molecular Conformation
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Molecular Weight
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Phosphates / analysis
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Phosphoenolpyruvate / metabolism*
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Phosphotransferases / metabolism*
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Polysaccharides, Bacterial / analysis*
Substances
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Bacterial Proteins
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Carbohydrates
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Glucans
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Phosphates
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Polysaccharides, Bacterial
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Phosphoenolpyruvate
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Phosphotransferases