Skip Navigation

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 Email this article to a friend
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 Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by MIZUNO, T.
Right arrow Articles by KAGEYAMA, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by MIZUNO, T.
Right arrow Articles by KAGEYAMA, M.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

J. Biochem, 1982, Vol. 91, No. 1 19-24
© 1982 Japanese Biochemical Society

research-article

The Peptidoglycan-Associated Lipoprotein (PAL) of the Proteus mirabilis Outer Membrane: Characterization of the Peptidoglycan-Associated Region of PAL

Takeshi MIZUNO1, Ritsuko KAGIYAMA and Makoto KAGEYAMA

Mitsubishi-Kasei Institute of Life Sciences Minamiooya, Machida, Tokyo 194

The peptidoglycan-associated lipoprotein (PAL) is present in the cell envelope in a form closely, but not covalently, associated with peptidoglycan in various Gramnegative bacteria. When the cell envelope or the isolated peptidoglycan-PAL complex from Proteus mirabilis, in which PAL maintains the interaction with peptidoglycan, was digested with trypsin, a polypeptide fragment with molecular weight 11,000 (11 K-fragment) was obtained. However, when isolated PAL or the 11 K-fragment which had been dissociated from peptidoglycan was treated with trypsin, they were further digested. The 11 K-fragment maintained essentially the same tight interaction with peptidoglycan as intact PAL. These results indicate that the 11 K-fragment is probably derived from the peptidoglycan-associated region of the PAL molecule. The purified 11 K-fragment contained neither covalently-linked fatty acid nor glycerylcysteine, which are known to be present at the N-terminus of PAL. The N-terminal sequence of the 11 K-fragment was also determined.

1 Present address: Department of Biochemistry, State University of New York at Stony Brook, N.Y. 11794, U.S.A.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J. Bacteriol.Home page
M. A. de Pedro, C. G. Grunfelder, and H. Schwarz
Restricted Mobility of Cell Surface Proteins in the Polar Regions of Escherichia coli
J. Bacteriol., May 1, 2004; 186(9): 2594 - 2602.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.