Characterization of the cell wall and cell wall proteins of Chromatium vinosum.

Journal of Bacteriology
B C Lane, R F Hurlbert

Abstract

Highly purified cell walls of Chromatium vinosum were isolated by differential centrifugation, with or without Triton X-100 extraction. The isolated material had a protein composition similar to that of cell walls obtained by sucrose density gradient centrifugation. Twenty-two proteins were reproducibly detected by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. A 42-kilodalton protein was shown to account for 65% of the total cell wall protein. The majority of cell wall proteins were solubilized in sodium dodecyl sulfate at room temperature; however, they existed as high-molecular-weight complexes unless heated to 45 degrees C or above. The cell wall contained one heat-modifiable protein which migrated with an apparent molecular weight of 37,400 when solubilized at 70 degrees C or below, but which migrated with an apparent molecular weight of 52,500 if solubilized at 100 degrees C. The electrophoretic mobility of three proteins was modified by 2-mercaptoethanol. The majority of C. vinosum cell wall proteins had isoelectric points between pH 4.5 and 5.5, and the 42-kilodalton protein focused at pH 4.9. No proteins were detected which were analogous to the lipoprotein or peptidoglycan-associated proteins of the Entero...Continue Reading

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Citations

Sep 1, 1988·Applied and Environmental Microbiology·J E StrayR E Hurlbert
May 1, 1983·Journal of Bacteriology·W J Newhall, R B Jones
Jan 1, 1986·Comparative Biochemistry and Physiology. B, Comparative Biochemistry·A G SpiesK D Spence
Jul 1, 1984·Journal of Bacteriology·H T Flammann, J Weckesser
Jul 1, 1984·Journal of Bacteriology·H T Flammann, J Weckesser
Jun 13, 1986·Biochemical and Biophysical Research Communications·M F MinnickK D Spence

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