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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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