Abstract |
Cell wall lytic enzyme ( Kyowa lytic no. 2 enzyme) liberated arthritogenic hydrosoluble peptidoglycans from both arthritogenic and non-arthritogenic bacterial cell walls. From these cell walls, mutanolysin ( peptidoglycan-degrading enzyme) also liberated hydrosoluble peptidoglycans which, however, lacked arthritogenicity. Based on the chemical composition of these peptidoglycans, it was suggested that their arthritis-inducing ability depends on a relatively long chain of glycan units that consists of repeated units of N-acetylglucosaminyl- N-acetylmuramic acid. However, the glycan chain lengths on these peptidoglycans appeared to be related to their adjuvancy rather than to an antigen(s) responsible for development of arthritis in rats.
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Authors | O Kohashi, C M Pearson, Y Watanabe, S Kotani |
Journal | Infection and immunity
(Infect Immun)
Vol. 16
Issue 3
Pg. 861-6
(Jun 1977)
ISSN: 0019-9567 [Print] United States |
PMID | 302240
(Publication Type: Comparative Study, Journal Article, Research Support, U.S. Gov't, P.H.S.)
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Chemical References |
- Peptidoglycan
- Water
- Squalene
- Endopeptidases
- Kyowa lytic no. 2 enzyme
- mutanolysin
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Topics |
- Animals
- Arthritis, Experimental
(chemically induced)
- Bacteria
(analysis)
- Cell Wall
(analysis, metabolism)
- Endopeptidases
(metabolism)
- Female
- Hypersensitivity, Delayed
(chemically induced)
- Peptidoglycan
(adverse effects, isolation & purification, metabolism)
- Rats
- Rats, Inbred Lew
- Solubility
- Species Specificity
- Squalene
- Water
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