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. 2003 Jan;71(1):335–342. doi: 10.1128/IAI.71.1.335-342.2003

TABLE 3.

Characterization of T. denticola GGTa

Treatment Conditions Enzyme activity (% of control)
GGT Cystalysin
Control Buffer only 100.0 ± 5.6 100.0 ± 5.6
Proteinase inhibitor 100 μg/ml
    TLCK 2 mM 5.8 ± 0.5 96.8 ± 10.2
    PMSF 2 mM 95.8 ± 5.8 98.4 ± 8.8
    Benzamidine 2 mM 98.5 ± 8.9 95.5 ± 6.7
Thiol compound
    2-ME 6 mM 255.1 ± 16.8 189.5 ± 12.6
    l-Cysteine 6 mM 155.9 ± 13.7 ND
    Dithiothreitol 6 mM 219.8 ± 18.9 168.9 ± 8.6
Proteinase
    Proteinase K 100 μg/ml 4.9 ± 0.6 91.8 ± 7.6
    Pronase 100 μg/ml 15.4 ± 1.8 95.4 ± 8.9
Salt
    NaCL 600 mM 105.8 ± 9.6 101.5 ± 12.4
    KCL 600 mM 155.6 ± 8.9 98.4 ± 10.2
Heating 56°C 20.5 ± 2.1 92.5 ± 8.9
Freezing −20°C 98.5 ± 6.8 100.5 ± 11.9
a

Purified recombinant GGT and cystalysin of T. denticola were compared with regard to their sensitivities to various treatments. Significant differences between the two enzymes in their sensitivities to TLCK, proteinase, heating, and KCl treatment are shown. ND, not determined.