Dodecyl sulfide

First, a general method of transformation of the expression plasmid into E. coli will be described, as well as appropriate conditions for growth and induction of the expression cultures. Then, the 96-well protein purification method is detailed. Last, analysis of the purified proteins is described using both lab-on-a-chip technology and traditional sodium dodecyl sulfide (SDS)-polyacryla-mide gel electrophoresis (PAGE). 

Fig. 1. Purified proteins imaged using (A) Agilent 2100 Bioanalyzer and (B) traditional sodium dodecyl sulfide-polyacrylamide gel electrophoresis. (A) Note that the lowest two bands and the uppermost band are internal standards for sizing and quantitation. (B) 3-15% polyacrylamide gel stained with GelCode Blue. In both panels, the predicted size of the protein is labeled at the top of each lane.

Fig. 4. Massive production of green fluorescent protein (GFP) by the continuous-flow cell-free method. Sodium dodecyl sulfide-polyacrylamide gel electrophoresis analysis of GFP produced during 14 d of reaction. mRNA produced by transcription of circular plasmid of Ehime University (pEU) was used for the translation reaction in the dialysis membrane system and was added every 48 h. A 0.1 -pL aliquot of the mixture was run on the gel and protein bands were stained with Coomassie Brilliant Blue. The arrow shows GFP and st designates an authentic GFP band (0.5 pg).

Fig. 7. Activity and folding of the cell-free produced polypeptides. Autophosphorylation activity of fixsArabidopsis protein kinases. Sodium dodecyl sulfide-polyaciy-lamide gel electrophoresis and Coomassie Brilliant Blue-stained gel of the partially purified products marked with asterisks (A), and the autoradiogram (B). Lanes 1-6 represent Atlg07150, At5g49760, At2g02800, At5g62710, and At4g35500, respectively. NC denotes samples from the reaction mixture incubated in the absence of mRNA. M protein size marker. Note that product of Atlg07150 (lane 1) did not show activity.

C15H32S propyl dodecyl sulfide 66271-82-7 583.00 62.104 2 29155 C16H140 methyl styrylphenyl ketone 1322-90-3 615.65 55.100 2... 

C15H32S propyl dodecyl sulfide 66271-82-7 284.16 38.736 2 29732 C16H3202 2-ethylhexyl-2-ethylhexanoate 7425-14-1 271.22 13.824 2... 

C16H34S butyl dodecyl sulfide 16900-08-6 288.16 41.326 2 30370 C17H37N methyl hexadecylamine 13417-08-8 309.15 44.795 2... 

C12H10O diphenyl ether 101-84-8 1.126E-h10 95.380 26551 C13H28S methyl dodecyl sulfide. .. 2.039E+10 150.670... 

C12H20O4 dibutyl maleate 105-76-0 1.890E-t-10 136.060 27950 C14H30S ethyl dodecyl sulfide 2851-83-4 2.174E-h10 160.900... 

C15H32S propyl dodecyl sulfide 66271-82-7 2.309E+10 171.130 31155 C18H38S propyl pentadecyl sulfide 66292-32-8 2.714E-K10 201.820... 

C16H34S butyl dodecyl sulfide 16900-08-6 2.444E+10 181.360 32399 C20H34 1 -phenyltetradecane 1459-10-5 2.567E+10 195.060... 

FIGURE 5.9 Effect of di-n-dodecyl sulfide on the oxidation stability of a desulfurized base stock and its (A + H) and (N + P) fractions. 

Figure 9.1.1 Combinatorial peptide libraries as obtained by Merrifield synthesis of peptides on membrane-covered gold particles allow not only investigations of recognition processes between the surface receptors and water-soluble substrates. Systematic changes of the environment of the receptor also become feasible (see Secs. 9.3.2 and 9.6.10). Steps I, III, and V are coupling reactions steps II, IV, and VI are deprotection reactions. About 50 thiolate molecules, including dodecyl sulfide and three peptides, have been deposited on a single gold cluster in statistical distributions and arrangements. (From Templeton et al., 1998.)...

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