Chorismate mutase-prephenate dehydrogenase from Escherichia coli. Purification and properties of the bifunctional enzyme.
Sampathkumar, P
Chorismate mutase-prephenate dehydrogenase from Escherichia coli. Purification and properties of the bifunctional enzyme. [electronic resource] - Biochimica et biophysica acta Apr 1982 - 204-11 p. digital
Publication Type: Journal Article
0006-3002
10.1016/0167-4838(82)90504-0 doi
Amino Acids--analysis
Drug Stability
Escherichia coli--enzymology
Isoelectric Point
Kinetics
Molecular Weight
Oxidoreductases--isolation & purification
Prephenate Dehydrogenase--isolation & purification
Spectrophotometry, Ultraviolet
Trypsin
Ultracentrifugation
Chorismate mutase-prephenate dehydrogenase from Escherichia coli. Purification and properties of the bifunctional enzyme. [electronic resource] - Biochimica et biophysica acta Apr 1982 - 204-11 p. digital
Publication Type: Journal Article
0006-3002
10.1016/0167-4838(82)90504-0 doi
Amino Acids--analysis
Drug Stability
Escherichia coli--enzymology
Isoelectric Point
Kinetics
Molecular Weight
Oxidoreductases--isolation & purification
Prephenate Dehydrogenase--isolation & purification
Spectrophotometry, Ultraviolet
Trypsin
Ultracentrifugation