Literature DB >> 8588916

Single-step purification of a thermostable DNA polymerase expressed in Escherichia coli.

U J Desai1, P K Pfaffle.   

Abstract

The coding region of the gene for Taq DNA polymerase has been cloned into the common vector pUC18. Using a single-step procedure, large amounts of active enzyme can be purified from Escherichia coli carrying this construct. This procedure takes advantage of the thermostable properties of the DNA polymerase. This simple procedure gives very high yields of essentially homogeneous, highly active enzyme suitable for use in molecular biological applications. Yields are over two orders of magnitude greater than available with current methods.

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Year:  1995        PMID: 8588916

Source DB:  PubMed          Journal:  Biotechniques        ISSN: 0736-6205            Impact factor:   1.993


  18 in total

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5.  Cloning, mutagenesis, and structural analysis of human pancreatic alpha-amylase expressed in Pichia pastoris.

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7.  A novel approach for high-level expression and purification of GST-fused highly thermostable Taq DNA polymerase in Escherichia coli.

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10.  Optimization of Taq DNA polymerase enzyme expression in Escherichia coli.

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