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Translate More Protein with Higher Biological Activity

vity (data not shown), suggesting that the proteins synthesized were either not full length or not fully functional.

Figure 4. Specific Activity of Proteins Synthesized Using the ActivePro Kit. DNA template (1 g) for -galactosidase (-gal) (A) or rhodanese (B) was used in either an ActivePro Kit reaction or another commercially available E.coli lysate kit according to protocol. Each reaction included 20 Ci 35S-labeled methionine. Each reaction (1 l) along with native -gal (Sigma) was assayed for by colorimetric ONGP hydrolysis assay. Rhodanese was assayed by the colorimetric assay described by Sorbo1. Yield was assayed by TCA precipitation and specific activity was calculated. The specific activity of rhodanese is as reported by Kudlicki2.

Figure 5 . Yields of Both Prokaryotic and Eukaryotic Proteins. DNA templates (1-2 ug) to several prokaryotic and eukaryotic proteins were in vitro transcribed/translated using 20 Ci 35 S-labeled methionine for 1 hour at 37C according to the ActivePro protocol. 5 l of each reaction was assessed on an SDS-PAGE gel and exposed overnight to film.


Efficient Synthesis of Many Prokaryotic and Eukaryotic Proteins
During development of an in vitro translation system, the lysate is optimized to translate the protein(s) used for testing; this is often the "control" provided in a commercially available kit. However, excellent translation of the control does not necessarily mean that the translation system will give the same yields for ot
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