Chemical synthesis and expression of a gene coding for bovine liver phosphotyrosine-protein phosphatase.
A chemically synthesized polynucleotide sequence coding for bovine liver low molecular weight acid phosphatase (which possesses phosphotyrosine-protein phosphatase activity) has been cloned in a E. coli expression vector. The recombinant protein retains correct affinity for substrate and inhibitors but shows a reduced specific activity.
Raugei
G
G
Department of Biochemical Sciences, University of Florence, Italy.
Marzocchini
R
R
Modesti
A
A
Ratti
G
G
Cappugi
G
G
Camici
G
G
Manao
G
G
Ramponi
G
G
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002417:Cattle; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000378:metabolism*; D015870:Gene Expression; D005813:Genes, Synthetic; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D008969:Molecular Sequence Data; D010749:Phosphoprotein Phosphatases / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D017027:Protein Tyrosine Phosphatases; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D013379:Substrate Specificity
D011994:Recombinant Proteins; D010749:Phosphoprotein Phosphatases; D017027:Protein Tyrosine Phosphatases