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. 2005 Jun;138(2):1046–1057. doi: 10.1104/pp.104.057406

Figure 1.

Figure 1.

Purification of TPPII from Arabidopsis seedlings. A, SDS-PAGE analysis of the TPPII purification steps. Samples from the crude extract, 2% to 8% PEG precipitation, pooled fractions from the UnoQ anion-exchange column, and the peak fraction from the Superose HR6 column were subjected to SDS-PAGE and silver staining. Positions of the 153- and 142-kD TPPII species are indicated. B and C, Elution profile of TPPII during size exclusion chromatography. The TPPII-containing fractions from UnoQ FPLC (lane C, left) were subjected to FPLC on a HR6 Superose column. B, TPPII peptidase activity using AAF-AMC as the substrate of the fractions with (□) and without (▪) the addition of 50 μm butabindide. Elution profile of total protein (A280) is included. C, SDS-PAGE of the column fractions surrounding the peak of TPPII peptidase activity. The positions of the 153- and 142-kD forms of TPPII are shown. The SDS-PAGE migration and elution position of the heat shock protein-60 chaperonin and the 20S CP of the 26S proteasome are indicated in B and C.