Separation of ribosomal proteins from Escherichia coli and rabbit reticulocytes using reverse-phase high-performance liquid chromatography

Biochemistry ◽  
1984 ◽  
Vol 23 (15) ◽  
pp. 3434-3442 ◽  
Author(s):  
Robert J. Ferris ◽  
Cynthia A. Cowgill ◽  
Robert R. Traut
2005 ◽  
Vol 187 (4) ◽  
pp. 1287-1292 ◽  
Author(s):  
Tatsuya Fukushima ◽  
Toshihiko Kitajima ◽  
Junichi Sekiguchi

ABSTRACT A polysaccharide deacetylase homologue, PdaA, was determined to act as an N-acetylmuramic acid deacetylase in vitro. Histidine-tagged truncated PdaA (with the putative signal sequence removed) was overexpressed in Escherichia coli cells and purified. Measurement of deacetylase activity showed that PdaA could deacetylate peptidoglycan treated with N-acetylmuramoyl-l-alanine amidase CwlH but could not deacetylate peptidoglycan treated with or without dl-endopeptidase LytF (CwlE). Reverse-phase high-performance liquid chromatography and mass spectrometry (MS) and MS-MS analyses indicated that PdaA could deacetylate the N-acetylmuramic acid residues of purified glycan strands derived from Bacillus subtilis peptidoglycan.


1986 ◽  
Vol 153 (2) ◽  
pp. 230-234 ◽  
Author(s):  
Koon-Sea Hui ◽  
Maria Hui ◽  
Fung-Chow Chiu ◽  
Miriam Banay-Schwartz ◽  
Teresita Deguzman ◽  
...  

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