Preparation of arthritogenic hydrosoluble peptidoglycans from both arthritogenic and non-arthritogenic bacterial cell walls.
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.
D000818:Animals; D001169:Arthritis, Experimental / Q000139:chemically induced; D001419:Bacteria / Q000032:analysis*; D002473:Cell Wall / Q000032:analysis / Q000378:metabolism; D010450:Endopeptidases / Q000378:metabolism; D005260:Female; D006968:Hypersensitivity, Delayed / Q000139:chemically induced; D010457:Peptidoglycan / Q000009:adverse effects / Q000302:isolation & purification* / Q000378:metabolism; D051381:Rats; D011917:Rats, Inbred Lew; D012995:Solubility; D013045:Species Specificity; D013185:Squalene; D014867:Water
D010457:Peptidoglycan; D014867:Water; D013185:Squalene; D010450:Endopeptidases; C021483:Kyowa lytic no. 2 enzyme; C021816:mutanolysin