isopropyl-thiogalactoside and glyoxylic-acid

isopropyl-thiogalactoside has been researched along with glyoxylic-acid* in 1 studies

Other Studies

1 other study(ies) available for isopropyl-thiogalactoside and glyoxylic-acid

Article	Year
The expression of spinach glycolate oxidase (GO) in E. coli and the application of GO in the production of glyoxylic acid. Molecular biotechnology, 2003, Volume: 25, Issue:3 The complementary deoxyribonucleic acid (cDNA) coding spinach glycolate oxidase (GO) was amplified by reverse transcription polymerase chain reaction (RT-PCR), using the total ribonucleic acid (RNA) of spinach leaves as the template, and was cloned into cloning vector pMD18-T. After the DNA sequence was determined, the go gene was subcloned into Escherichia coli expression vectors. Sodium dodecyl sulfatepolyacrylamide gel electrophoresis (SDS-PAGE) analysis showed that recombinant GO was expressed in E. coli BL21 (DE3)(pTIG-Trx-GO) and E. coli BL21 (DE3)(pET-22b(+)-GO). The result of the enzyme activity assay and the oxidation of glycolate to glyoxylate catalyzed by the whole cells of E. coli BL21 (DE3)(pET- 22b(+)-GO) proved the feasibility of using E. coli cells to produce glyoxylic acid. Topics: Alcohol Oxidoreductases; Cloning, Molecular; DNA Primers; DNA, Complementary; Escherichia coli; Gene Expression Regulation, Plant; Genetic Vectors; Glyoxylates; Isopropyl Thiogalactoside; Plasmids; Polymerase Chain Reaction; Recombinant Fusion Proteins; Recombinant Proteins; Spinacia oleracea	2003

Article

Year

The expression of spinach glycolate oxidase (GO) in E. coli and the application of GO in the production of glyoxylic acid.

Molecular biotechnology, 2003, Volume: 25, Issue:3

The complementary deoxyribonucleic acid (cDNA) coding spinach glycolate oxidase (GO) was amplified by reverse transcription polymerase chain reaction (RT-PCR), using the total ribonucleic acid (RNA) of spinach leaves as the template, and was cloned into cloning vector pMD18-T. After the DNA sequence was determined, the go gene was subcloned into Escherichia coli expression vectors. Sodium dodecyl sulfatepolyacrylamide gel electrophoresis (SDS-PAGE) analysis showed that recombinant GO was expressed in E. coli BL21 (DE3)(pTIG-Trx-GO) and E. coli BL21 (DE3)(pET-22b(+)-GO). The result of the enzyme activity assay and the oxidation of glycolate to glyoxylate catalyzed by the whole cells of E. coli BL21 (DE3)(pET- 22b(+)-GO) proved the feasibility of using E. coli cells to produce glyoxylic acid.

Topics: Alcohol Oxidoreductases; Cloning, Molecular; DNA Primers; DNA, Complementary; Escherichia coli; Gene Expression Regulation, Plant; Genetic Vectors; Glyoxylates; Isopropyl Thiogalactoside; Plasmids; Polymerase Chain Reaction; Recombinant Fusion Proteins; Recombinant Proteins; Spinacia oleracea

2003