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. 2002 Mar;128(3):1149. doi: 10.1104/pp.010612

Table V.

Effects of MCO on the three peptidic activities of 20S proteasomes isolated from starved and non-starved maize root tips

20S Proteasome Chymotrypsin Like Trypsin Like PGPH
nmol mg−1 h−1
T0
 Nonoxidized 104 ± 3 204 ± 8 54 ± 5
 Oxidized 220 ± 7 140 ± 12 67 ± 1
T24 starved
 Nonoxidized 192 ± 0 159 ± 15 58 ± 9
 Oxidized 162 ± 1 124 ± 8 45 ± 1
T24 + Glc
 Nonoxidized 124 ± 3 185 ± 7 42 ± 6
 Oxidized 237 ± 4 154 ± 8 77 ± 12

Isolated 20S proteasomes from T0, T24-starved, and T24 + Glc root tips were oxidized for 3 h at 37°C in the presence of Fe2+/ascorbate. Control proteasomes (nonoxidized) were incubated in parallel without Fe2+/ascorbate. Peptidic activities of oxidized and nonoxidized proteasomes were then measured as described in “Materials and Methods.” Values are the mean of six measurements from three independent experiments.