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. 2005 Jun;187(12):4140–4148. doi: 10.1128/JB.187.12.4140-4148.2005

TABLE 1.

Summary of purification of Pz peptidases A and B

Purification step Total protein (mg) Sp act (U/mg protein) Fold Total activity (U) Yield (%)
Pz peptidase A
    1. Cell-free extract 7,370 0.045 1 332 100
    2. Ammonium sulfate fractionation 2,120 0.101 2.24 214 64.5
    3. DEAE cellulose 1,150 0.161 3.58 185 55.7
    4. Butyl-TOYOPEARL 650S 91.5 0.798 17.7 73.0 22.0
    5. 1st Sephadex G-200 11.8 4.91 109 57.9 17.4
    6. 2nd Sephadex G-200 4.42 9.76 217 43.1 13.0
    7. DEAE Sepharose CL-6B 1.66 18.4 409 30.5 9.2
    8. 3rd Sephadex G-200 0.92 24.7 549 22.7 6.8
Pz peptidase B
    1. Cell-free extract 5,890 0.0477 1 281 100
    2. (NH4)2SO4 fractionation 3,230 0.0845 1.77 273 97.2
    3. DEAE cellulose 1,530 0.144 3.01 220 78.3
    4. DEAE Sepharose CL-6B 225 0.267 5.60 60.0 21.3
    5. 2nd DEAE Sepharose CL-6B 94.9 0.363 7.09 34.5 12.3
    6. Sephadex G-200 67.9 0.481 10.1 32.7 11.6
    7. Butyl-TOYOPEARL 650S 29.3 0.345 7.23 10.1 3.6
    8. Phenyl Sepharose CL-4B 11.2 0.730 15.3 8.18 2.9
    9. Ethyl agarose 5.93 1.45 30.4 8.60 3.1
    10. Sephacryl S-300 2.35 2.32 48.6 5.45 1.9