Article Abstract:
Purification, mutant studies and gene cloning relative to ferritin from the obligate anaerobe Porphyromonas gingivalis, an obligate anaerobe, are discussed. The organism cane store heme on its cell surface, which gives black pigmentation of colonies on blood agar plates. Not much is known about its intracellular iron storage. P. gingivalis ferritin was found to comprise non-heme iron.
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Article Abstract:
Arg-X specific protease activity in the Porphyromonas gingivalis mutant lacking Lys-X specific protease is similar to that of the wild type. The Lys-X protease is not involved in the generation of the Arg-X but its absence affects the release/transport of the Arg-X specific protease into the growth medium.
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Article Abstract:
Porphyromonas gingivalis is implicated as a cause of chronic adult periodontal disease. Proteases of P gingivalis are thought to be important in the virulence of the organism. Arg-specific proteases produced by the avirulent W50/BE1 strain were purified and characterized, and significant differences were seen between the P. gingivalis proteases W50 and W50/BE1. It is suggested that reduced extracellular protease activity in W50/BE1 reflects reduced synthesis.
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