JB
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Hengstenberg, W.
Right arrow Articles by Morse, M. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hengstenberg, W.
Right arrow Articles by Morse, M. L.

 Previous Article  |  Next Article 

J Bacteriol. 1969 August; 99(2): 383-388
Copyright © 1969 American Society for Microbiology. All Rights Reserved.

Phosphotransferase System of Staphylococcus aureus: Its Requirement for the Accumulation and Metabolism of Galactosides

Wolfgang Hengstenberg, W. K. Penberthy, Katherine L. Hill and M. L. Morse

Webb-Waring Institute for Medical Research, and the Department of Biophysics, University of Colorado Medical Center, Denver, Colorado 80220

ABSTRACT

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-ß-D-galactoside-6-phosphate by the system and its hydrolysis by the staphylococcal 6-phospho-ß-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-ß-galactosidase, 45,000. Enzyme II is a membrane-bound protein.

J Bacteriol. 1969 August; 99(2): 383-388
Copyright © 1969 American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:



Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
Appl. Environ. Microbiol. Infect. Immun. Eukaryot. Cell
Mol. Cell. Biol. J. Virol. Microbiol. Mol. Biol. Rev.
ALL ASM JOURNALS

Copyright © 1969 by the American Society for Microbiology. All rights reserved.