Synthese von [32P]phosphoenolpyruvat.
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Biomedical subjects
Publications and source records attributed to W Hengstenberg.
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The membrane bound lactose specific component of the PEP dependant phosphotransferase system of Staphylococcus aureus has been solubilized using the non ionic detergent Triton X-100. Some properties of the crude soluble enzyme are reported.
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The phosphotransferase system of Staphylococcus aureus was characterized. Mutants defective in enzyme I and heat-stable (HPr) protein as well as in the two components specific to lactose accumulation, factor III and enzyme II, were isolated. Colorimetric assays for each of the components are presented based on the formation of o-nitrophenyl-beta-d-galactoside-6-phosphate by the system and its hydrolysis by the staphylococcal 6-phospho-beta-galactosidase. The components were partially purified and their molecular weights were estimated: enzyme I, 100,000 +/- 15%; HPr, 10,000 +/- 15%; factor III, 30,000 +/- 15%; 6-phospho-beta-galactosidase, 45,000. Enzyme II is a membrane-bound protein.
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THE METABOLISM OF LACTOSE WAS FOUND TO BE CONTROLLED BY THREE GENES: a gene for the synthesis of a beta-galactosidase attacking only phosphorylated galactosides; a gene for a protein permitting concentration of phosphorylated galactosides which probably acts by transferring phosphates to them; and a gene regulating the first two structural genes. The three genes are closely linked and may have the same order as in Escherichia coli. Galactose-6-phosphate was found to be a better inducer of lactose utilization than is galactose or any other inducer. The inhibition of induction by isopropylthiogalactoside was found to occur at the level of the protein permitting the concentration of galactoside phosphates.
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