3.4.21.92 23000 - 240000 (ClpP with the subunit structure 12 * 23000, SDS-PAGE), gel filtration in presence of more than or at 0.1 M KCl, in absence of KCl, native ClpP appears to dimerize giving a structure with a MW of 500000 29857 3.4.21.92 240000 - 240000 (ClpP with the subunit structure 12 * 23000, SDS-PAGE), gel filtration in presence of more than or at 0.1 M KCl, in absence of KCl, native ClpP appears to dimerize giving a structure with a MW of 500000 29857 3.4.21.92 21000 - 1 * 230000, subunit ClpP (12 * 21000, amino acid sequence, subunit of ClpP) 29858 3.4.21.92 83000 - x * 120000-140000, subunit ClpA, gel filtration, x * 83000, subunit ClpA, amino acid sequence 29858 3.4.21.92 230000 - 1 * 230000, subunit ClpP (12 * 21000, amino acid sequence, subunit of ClpP) 29858 3.4.21.92 23000 - x * 80000 (ClpA, SDS-PAGE, behaves as a dimer of MW 140000 Da on gel filtration) + x * 23000 (ClpP, SDS-PAGE, behaves as a complex of 10-12 subunits, MW 260000 Da) 29860 3.4.21.92 80000 - x * 80000 (ClpA, SDS-PAGE, behaves as a dimer of MW 140000 Da on gel filtration) + x * 23000 (ClpP, SDS-PAGE, behaves as a complex of 10-12 subunits, MW 260000 Da) 29860 3.4.21.92 340000 - E. coli 29860 3.4.21.92 81000 - x * 81000, ClpA, SDS-PAGE 29862 3.4.21.92 46000 - x * 46000, ClpX, SDS-PAGE 29865 3.4.21.92 46300 - x * 46300, ClpX, calculation from amino acid sequence 29866 3.4.21.92 700000 - E. coli, complex of subunits ClpA with ClpP in presence of ATP 29867 3.4.21.92 22000 - ClpP1(pClpP), MALDI-TOF, ClpS1(nClpC like), MALDI-TOF, ClpP5 (nClpP1), MALDI-TOF, ClpP6 (nClpP6), MALDI-TOF 652115 3.4.21.92 23000 25000 ClpP2 (nClpP7), MALDI-TOF 652115 3.4.21.92 26000 - ClpR2 (nClpP2), MALDI-TOF, 6,13,21 ClpP4 (nClpP4), MALDI-TOF 652115 3.4.21.92 27000 - ClpR3 (nClpP8), MALDI-TOF 652115 3.4.21.92 28000 - ClpR1 (nClpP5), MALDI-TOF 652115 3.4.21.92 29000 - ClpP3 (nClpP3), MALDI-TOF 652115 3.4.21.92 350000 - ClpP protease complex, gel filtration 652115 3.4.21.92 26000 29000 2 isoenzymes, immunoblot analysis, antibody against plastid-encoded rice ClpP 653568 3.4.21.92 12620 - ClpA, analytical ultracentrifugation 653631 3.4.21.92 12640 - ClpB, analytical ultracentrifugation 653631 3.4.21.92 13940 - ClpX, analytical ultracentrifugation 653631 3.4.21.92 14230 - ClpY, analytical ultracentrifugation 653631 3.4.21.92 300000 - - 683473 3.4.21.92 140000 - native Page, ClpP1 683643 3.4.21.92 140000 - native Page, ClpP2 683643 3.4.21.92 270000 - native Page, ClpP3 and ClpPR 683643 3.4.21.92 300000 - gel filtration, ClpP1 and ClpP2 683643 3.4.21.92 180000 - n * 230000, n * 180000, ClpP1, ClpP3, clpP4, ClpP5, clpP6, clpR1, clpR2, ClpR3, cClR4, ClpS1 683977 3.4.21.92 230000 - n * 230000, n * 180000, ClpP1, ClpP3, clpP4, ClpP5, clpP6, clpR1, clpR2, ClpR3, cClR4, ClpS1 683977 3.4.21.92 335000 - wild type, native Page, decreased by 80% in clpP6 antisense mutants, ClpP6 is necessary for the formation of the Clp proteolytic core complex 683977 3.4.21.92 270000 - native-PAGE 698890 3.4.21.92 25000 - Western blot 717993 3.4.21.92 43000 - calculated from cDNA, unprocessed protein 717993 3.4.21.92 300000 - gel filtration 718406 3.4.21.92 346000 - sedimentation velocity analytical ultracentrifugation, tetradecamer 718406 3.4.21.92 150000 - gel filtration, enzyme treated with inhibitor diisopropyl fluorophosphate, 1-[4-(4-ethynylbenzoyl)-1,1-dioxido-1,2-thiazetidin-2-yl]undec-10-en-1-one, or beta-lactone (4R)-3-(4-methoxyphenyl)-4-(pent-4-yn-1-yl)oxetan-2-one 731985 3.4.21.92 304000 - gel filtration, native enzyme 731985 3.4.21.92 300000 - gel filtration, assembled double-ring complex 755086