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Results: 5

1.
Figure 5

Figure 5. From: Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm.

Plasminogen activation in lysates of cells expressing vtPA secreted to the periplasm of DHB4 (wild type) or in the cytoplasm of FA113 (trxB gor supp). Foldases were coexpressed from plasmids pBADdsbA, pBADdsbC, pBADΔSSdsbA, pBADΔSSdsbC, pFA3, and pFA5.

Paul H. Bessette, et al. Proc Natl Acad Sci U S A. 1999 November 23;96(24):13703-13708.
2.
Figure 3

Figure 3. From: Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm.

Pulse–chase of alkaline phosphatase. Signal sequenceless alkaline phosphatase (AP) was immunoprecipitated and separated by native PAGE, such that the oxidized form (ox) was distinguished from the reduced form (red). Time is indicated in minutes postchase. Strains used were DHB4 (wild type), WP597 (trxB), and FA113 (trxB gor supp) transformed with plasmid pAID135. OmpA was used as an internal standard.

Paul H. Bessette, et al. Proc Natl Acad Sci U S A. 1999 November 23;96(24):13703-13708.
3.
Figure 2

Figure 2. From: Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm.

Growth curves of DHB4 (●); FA113 (■); FA113/pTrcvtPA/pFA5 (♦); and DHB4/pTrcStIIvtPA/pBADdsbC (▴) grown aerobically at 37°C in LB medium in test tubes. Expression of vtPA was induced at late log phase as described in the text. Optical density was measured in a microtiter plate reader.

Paul H. Bessette, et al. Proc Natl Acad Sci U S A. 1999 November 23;96(24):13703-13708.
4.
Figure 1

Figure 1. From: Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm.

tPA activity in DHB4 (wild type), WP597 (trxB), FA112 (trxB gshA supp), and FA113 (trxB gor supp) monitored by the fibrinolysis assay. Cells were transformed with plasmids pTrcvtPA, and pFA5 (bottom row only). Soluble protein (10 μg) from induced cultures was spotted onto fibrin/agarose plates and was incubated for 24 hr at 37°C. Clearance zones qualitatively measure biological activity of bacterially produced vtPA.

Paul H. Bessette, et al. Proc Natl Acad Sci U S A. 1999 November 23;96(24):13703-13708.
5.
Figure 4

Figure 4. From: Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm.

The effect of coexpression of vtPA and oxidoreductases in the cytoplasm of strain FA113 (trxB gor supp) quantified by an indirect assay for plasminogen activation using a chromogenic plasmin substrate (see text). Activity has been normalized to the value obtained from vtPA expressed alone in FA113 (column 1). Cell lysates used for columns 2–8 were from strains cotransformed with plasmids pFA2-pFA8, respectively. Plasmids pFA3–8 overexpress active site mutants of TrxA. The amino acid sequence of the active site is listed, along with the known oxidoreductase that contains that native active site.

Paul H. Bessette, et al. Proc Natl Acad Sci U S A. 1999 November 23;96(24):13703-13708.

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