Published September 1990
| Version v1
Journal article
Phosphorylated tyrosine in the flagellum filament protein of Pseudomonas aeruginosa
Description
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
Additional details
Publishing Information
- Journal Title
- Journal of Bacteriology
- Journal Volume
- 172
- Journal Issue
- 9
- Series
- J. Bacteriol.
- Journal Page Range
- 5135-5139
- ISSN
- 0021-9193
- CODEN
- JOBAA
INIS
- Country of Publication
- United States
- Country of Input or Organization
- United States
- INIS RN
- 22012020
- Subject category
- S60: APPLIED LIFE SCIENCES;
- Descriptors DEI
- AUTORADIOGRAPHY; ELECTROPHORESIS; LIQUID COLUMN CHROMATOGRAPHY; MOLECULAR WEIGHT; ORGANOIDS; PHOSPHORUS 32; PHOSPHORYLATION; PSEUDOMONAS; TYROSINE
- Descriptors DEC
- 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