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A polypeptide of expected molecular weight (Mr) was expressed at high levels upon induction using 1.0 mM IPTG (Fig. S1C).
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In tomato, a single polypeptide of 30 kDa was detected in leaf extract of the Hm-WT and as expected a polypeptide of approximatively 22 kDa corresponding to the mutant form was detected in Sl-eIF4E1 G1485A (Figure 4A).
SDS-PAGE analysis of MT-I and MT-II crude extracts from the transformed E. coli (M15) showed high amounts of a polypeptide with the expected molecular mass (ca. 6.5 and 8 kDa) (Figure 3A and 3B).
SDS-PAGE analysis of MT-I and MT-II crude extracts from the transformed E. coli (M15) showed high amounts of a polypeptide with the expected molecular mass (ca. 6.5 and 8 kDa, respectively) (Figure 1).
The protein was purified on glutathione-Sepharose to yield a polypeptide with the expected mass of 40 kDa.
As shown in Figure 2A, although there were some differences in the time course of expression, five of six of the yeast cell lines secreted a major methanol-dependent polypeptide of the expected size of the HSA fusion proteins, of 70-80 kDa.
The aleh1 encoded a polypeptide of 581 amino acids.
The ORF encoded a polypeptide of 581-amino acids (Figure 2).
The truncated protein could be a polypeptide of CD molecules or an epitope of mAbs, such as a truncated human EGFR polypeptide (huEGFRt) (Fig. 4) (Wang et al., 2011).
It contained an open reading frame encoding a polypeptide of 560 amino acids.
They encoded a polypeptide of 220 amino acid residues.
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