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Dental plaque deposits are known to be potent stimulants of lymphocyte transformation in patients with periodontal disease but not in normal subjects. Since plaque deposits consist mainly of whole bacteria, the cell walls of the most commonly found organisms in plaque were tested for their capacity to induce lymphocyte transformation. There was a direct correlation between the severity of peridontal disease and the amount of transformation induced by the cell walls of oral bacteria and by solubilized dental plaque. Cord blood leukocytes and lymphocytes from clinically normal people did not respond, which indicates that these stimulants are antigens rather than mitogens. Of the eleven bacteria tested, four members of the family Actinomycetaceae (Actinomyces viscosus, A. israelii, A. naeslundii, and Arachnia propionica), the related Propionibacterium acnes, and an anaerobic gram-negative anaerobic rod (27N). The high prevalence of the former organisms in the mature dental plaque that forms around the gingival crevice area and the potent efficacy with which they stimulate lymphocytes indicates that Actinomyces and certain gram-negative anaerobes may be important etiological agents in chronic periodontal inflammation in man.

We have demonstrated for the first time that N-cadherin switching occurs in higher grade PC and correlates significantly with increasing Gleason patterns. N-cadherin may be as a useful biomarker of aggressive PC.

The cobamide coenzyme dependent @-lysine mutase has been purified to homogeneity by fractionation with ammonium sulfate and chromatography on DEAE-cellulose, Sephadex G-150, and DEAE-Sephadex A-50. The native enzyme is a tetramer (mol wt 170,000) composed of two subunits of approximately 32,000 and two of approximately 52,000 daltons. The enzyme exhibits an absolute dependency on pyridoxal phosphate for activity. During isolation there is degradation of enzyme-bound cobamide coenzyme to hydroxy(adeny1)cobamide which is a strong inhibitor and remains tightly bound to the protein. Incubation with cobalamin coenzyme, Mg2+, a mercaptan, and pyridoxal phos-

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