Cloning, sequencing and functional expression of a DNA encoding pig cytosolic malate dehydrogenase: purification and characterization of the recombinant enzyme
Copyright policy )Cloning, sequencing and functional expression of a DNA encoding pig cytosolic malate dehydrogenase: purification and characterization of the recombinant enzyme
Using the polymerase chain reaction, DNA encoding cytosolic malate dehydrogenase (cMDH) has been cloned from a pig heart cDNA library. Large amounts of the enzyme (30 mg per litre of original culture) have been produced in Escherichia coli using an inducible expression vector (pKK223-3) in which the 5'-non-coding region of the gene was replaced with the tac promoter. The complete nucleotide sequence of the DNA is reported for the first time. The recombinant cMDH purified was shown to be identical to the native enzyme according to: chromatographic behaviour, isoelectric point, N-terminal amino acid sequence, and physiochemical and catalytic properties.
- University of Bristol United Kingdom
- University of Barcelona Spain
580, 570, DNA, Complementary, Base Sequence, Swine, Myocardium, Recombinant Fusion Proteins, Molecular Sequence Data, DNA, Cytosol, Malate Dehydrogenase, Escherichia coli, Animals, Amino Acid Sequence, Cloning, Molecular
580, 570, DNA, Complementary, Base Sequence, Swine, Myocardium, Recombinant Fusion Proteins, Molecular Sequence Data, DNA, Cytosol, Malate Dehydrogenase, Escherichia coli, Animals, Amino Acid Sequence, Cloning, Molecular
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