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AbstractAbstract
[en] Purified flagella from two strains of 32P-labeled Pseudomonas aeruginosa were shown to be phosphorylated. This was confirmed by autoradiography of flagellin protein in polyacrylamide gels. Thin-layer electrophoresis and autoradiography of flagellin partial hydrolysates indicated that phosphotyrosine was the major phosphorylated amino acid. High-pressure liquid chromatographic analysis confirmed the presence of phosphotyrosine in flagellum filament protein. Preliminary data indicated that less than one tyrosine per subunit was phosphorylated. No evidence was found for phosphorylation of serine or threonine. A function related to tyrosine phosphorylation has not been determined
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Journal Article
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AMINO ACIDS, AROMATICS, BACTERIA, BETA DECAY RADIOISOTOPES, BETA-MINUS DECAY RADIOISOTOPES, CARBOXYLIC ACIDS, CELL CONSTITUENTS, CHEMICAL REACTIONS, CHROMATOGRAPHY, DAYS LIVING RADIOISOTOPES, HYDROXY ACIDS, ISOTOPES, LIGHT NUCLEI, MICROORGANISMS, NUCLEI, ODD-ODD NUCLEI, ORGANIC ACIDS, ORGANIC COMPOUNDS, PHOSPHORUS ISOTOPES, RADIOISOTOPES, SEPARATION PROCESSES
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