Dodecyl /3-d-maltoside

Finally there are two very slow phases with lifetimes of 225 ms and 5.5 s, respectively. These phases have been attributed to P700 reduction by reductants present in the medium, as they are negligible and only observed in the absence of reduced DCIPH2. The PS-I complex prepared with -dodecyl-(3-D-maltoside ( 3-DM) shows very similar kinetic phases over the three time domains (not shown). Also,... 

An alternative approach to increasing proteomic coverage is based on the analysis of isolated intact mitochondrial protein complexes. One strategy is based on the use of sucrose density gradients to separate intact mitochondrial complexes solubilised with n-dodecyl- 3-D-maltoside (Hanson et al., 2001). Initially the proteins from the individual fractions were analysed by 2-DE. However, subsequently this approach has been coupled with 1-D SDS-PAGE and MALDI PMF analysis of tryptic digests of excised protein bands (Taylor et al., 2003). When applied to human heart mitochondria, this... 

Cells of Synechocystis PCC 6803 were grown and thylakoid membranes isolated as in (2). Membranes were extracted with 1 % (w/v) dodecyl-8-D-maltoside (B-DM), (stirring for 30 min.in the dark) followed by a centrifugation step to remove non-solubilized material. The supernatant fraction was layered onto sucrose-density gradients (8 - 32 % (w/v), containing 0.04 % 6-DM) and spun for 14 hrs at 150,000 g, yielding 3 colored bands ... 

In most of those studies, the PS-I-RC was applied to a DEAE-cellulose and the Triton was exchanged with Dodecyl-P-D-Maltoside as described in (26). Then, about 20-100 pi of the PS-I-RC solution, in a chlorophyll concentration of about 4 mg/ml, were placed in a crystallization dish with 1-5% PEG-6000 or IM KPi as precipitants. The precipitant concentration in the reservoir buffer outside the crystallization wells was 2-3 times that of the concentration in the protein solution. The dishes were well sealed and crystallization was allowed to occur at 4-25X via v r diffusion as described by Michel et al (15). 

The immobilization of trimeric LHCII is demonstrated in Fig. 13(B). After the nickel ion activation (5), a 1 pM solution of trimeric recombinant LHCII prepared in NaP + DM buffer (20 mM sodium phosphate, pH 7.4, 0.1 % (w/v) n-dodecyl-/ -D-maltoside) was introduced into the flow cell (1). For each cycle, the protein solution was incubated in the loop for 30 min, followed by buffer rinse (2), EDTA (3), and SDS (4) regeneration. EDTA was used to competitively chelate the nickel ions and break the linkage between NTA and Histidine. SDS, as mentioned in Section 4.2, was used to detach any remaining physically adsorbed proteins. As shown in Fig. 13(B), the immobilization/regeneration cycles from (1) to (5) can be well reproduced and the baseline after every cycle stabilized at a response close to the starting level. This indicates that the... 

Fig. 1. Peptide patterns of PSl. A. TRIS/glycine gel of MW markers [lane 1], acetone-precipitated PSl core [lane 2], PSl core [lane 3], and a 2nd-dimensional analysis of a dodecyl-maltoside gel of membranes, resolving a PSl green band (Bl) and a PS2 green band (B2). B. TRICINE gel of MW markers [lane 1], NaBr-washed PSl [lane 2], and Bl excised from a dodecyl maltoside gel. C. TRIS/glycine gel of Anacvstis membranes [lanes 1,2] and isolated PSl core [lanes 3,4]. D. TRICINE gel of Anacvstis PSl core in the absence [left] and presence [right] of 6 M urea.

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