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We then clamped the ends of the IV tubing and ethernet cable with straight Kelly clamps to contain the gel Figures 1 and 2. Figure 1 Supplies needed.
EDC-modified native TRP47, GST-TRP47, and GST-CterTRP47 migrated faster at about 37±3 kDa, 60±3 kDa, and 46±3 kDa, close to their true molecular masses, than the unmodified proteins that migrate at 47 kDa, 67 kDa, and 55 kDa in SDS-PAGE gel (Figures 4A, 4C and Table 4).
The number of cycles that was finally chosen is indicated next to the gel figures shown in the results section.
The quality of some of the gel figures are perfectly clear whilst some are poor, exacerbated when the document is printed.
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The molecular weights in kDa are given to the left of each gel figure.
The molecular weights in kDa of a protein standard (lane M) are given to the left of the gel figure.
It is showed in the agarose gel (Figure 4a) that the hairpin monomers have assembled to DNA polymers with different molecular weight and the efficiency of the polymerization is proportional to the initial concentration of PCR products.
PaXynG was detected as a 33-kDa band on a CBB stained SDS-PAGE gel (Figure 5b).
In this study, digestion reactions were performed to remove GST from glucagon and confirmed by Tris-Tricine gel (Figure 1C).
This was in agreement with the decrease in breaking force and deformation of surimi gel (Figure 1).
The quantitative results of labelling with 111In3+ showed a better correspondence with the results of the protein gel (Figure 5b).
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