By Richard D Smallwood
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Sirpiö et al. , dodecyl maltoside [DM] or digitonin). Subsequently, Coomassie G-250 dye is added to the sample. Coomassie dye introduces a negative charge to the protein complexes and, thus, enhances migration and reduces aggregation of the protein complexes during electrophoresis. The Coomassie dye is omitted from clear native gel electrophoresis, which is thus more suitable for in-gel catalytic activity assays and for detection and quantification of proteins tagged with fluorescent dyes. However, the lack of the negative charge often results to less efficient separation of the protein complexes than in blue native gels.
The components of the complex are separated by SDS–PAGE prior to in-gel tryptic digestion followed by identification by mass spectrometry. 36 C. Andrès et al. 4. Protocol for the purification of protein complexes composed of membrane-bound proteins. The short protocol stops at the dashed line. 2. 1. 8 (adjust pH with KOH). Soil: Rasenerde Top Dressing (Ricoter AG, Aarberg, Switzerland). 2. Purified human immunoglobulin G (HsIgG) (MP Biomedicals, Irvine, CA, USA). 1 M Na2CO3). Cyanogen bromide (CNBr)-activated sepharose 4B (GE Healthcare, Chalfont St.
And Nakai, M. (2009) A 1-megadalton translocation complex containing Tic20 and Tic21 mediates chloroplast protein import at the inner envelope membrane. Plant Cell 21, 1781–1797. Bruce, B. , and Keegstra, K. (1994) In vitro import of proteins into chloroplasts. In, Plant Molecular Biology Manual, Vol. , and Schilperoot, R. ) Kluwer Academic Publishers, Belgium, pp. 1–15. , Summer, E. , and Cline, K. (1999) Component specificity for the thylakoidal Sec and Delta pH-dependent protein transport pathways.