Structural Studies of Peptidoglycans inCampylobacterSpecies
Author:
Affiliation:
1. Central Research Laboratory; Akita University School of Medicine; Akita Akita 010 Japan
Publisher
Wiley
Subject
Virology,Immunology,Microbiology
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1348-0421.1992.tb02099.x/fullpdf
Reference15 articles.
1. Peptidoglycan of Legionella pneumophila: apparent resistance to lysozyme hydrolysis correlates with a high degree of peptide cross-linking;Amano;J. Bacteriol.,1983
2. Sensitivity of Coxiella burnetii peptidoglycan to lysozyme hydrolysis and correlation of sacculus rigidity with peptidoglycan-associated proteins;Amano;J. Bacteriol.,1984
3. Electron microscopic observation of coccoid form of Campylobacter lejuni and Campylobacter coli;Amano;Rinsho to Biseibutsu,1992
4. Electron microscopy of the coccoid form of Campylobacter jejuni;Buck;J. Clin. Microbiol.,1983
5. Chemical structure of peptidoglycan in Selenomonas ruminantium: cadaverine links covalently to the d-glutamic acid of peptidoglycan;Kamio;J. Bacteriol.,1981
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