Expression of rat hepatic glucokinase in Escherichia coli

C. T. Chien; A. Tauler; A. J. Lange; K. Chan; R. L. Printz; M. R. El-Maghrabi; D. K. Granner; S. J. Pilkis

doi:10.1016/S0006-291X(89)80039-7

Expression of rat hepatic glucokinase in Escherichia coli

C. T. Chien, A. Tauler, A. J. Lange, K. Chan, R. L. Printz, M. R. El-Maghrabi, D. K. Granner, S. J. Pilkis

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12 Scopus citations

Abstract

Rat Liver glucokinase was expressed in Escherichia coli by using an expression system based on bacteriophage T7 RNA polymerase. The expressed protein starts with the predicted initiator methionine residue and ends at the appropriate carboxyl terminal residue. It was partially purified by ammonium sulfate precipitation and gel filtration and had kinetic and physical properties similar to the purified rat liver enzyme. The efficient expression of this low abundance hepatic protein in bacteria provides a system for in vitro analysis of mutations of the enzyme.

Original language	English (US)
Pages (from-to)	817-825
Number of pages	9
Journal	Biochemical and Biophysical Research Communications
Volume	165
Issue number	2
DOIs	https://doi.org/10.1016/S0006-291X(89)80039-7
State	Published - Dec 15 1989
Externally published	Yes

Bibliographical note

Funding Information:
This work was supported by National Science Foundation Grant DMB 8608989

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10.1016/S0006-291X(89)80039-7

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title = "Expression of rat hepatic glucokinase in Escherichia coli",

abstract = "Rat Liver glucokinase was expressed in Escherichia coli by using an expression system based on bacteriophage T7 RNA polymerase. The expressed protein starts with the predicted initiator methionine residue and ends at the appropriate carboxyl terminal residue. It was partially purified by ammonium sulfate precipitation and gel filtration and had kinetic and physical properties similar to the purified rat liver enzyme. The efficient expression of this low abundance hepatic protein in bacteria provides a system for in vitro analysis of mutations of the enzyme.",

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note = "Funding Information: This work was supported by National Science Foundation Grant DMB 8608989",

year = "1989",

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doi = "10.1016/S0006-291X(89)80039-7",

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T1 - Expression of rat hepatic glucokinase in Escherichia coli

AU - Chien, C. T.

AU - Tauler, A.

AU - Lange, A. J.

AU - Chan, K.

AU - Printz, R. L.

AU - El-Maghrabi, M. R.

AU - Granner, D. K.

AU - Pilkis, S. J.

N1 - Funding Information: This work was supported by National Science Foundation Grant DMB 8608989

PY - 1989/12/15

Y1 - 1989/12/15

N2 - Rat Liver glucokinase was expressed in Escherichia coli by using an expression system based on bacteriophage T7 RNA polymerase. The expressed protein starts with the predicted initiator methionine residue and ends at the appropriate carboxyl terminal residue. It was partially purified by ammonium sulfate precipitation and gel filtration and had kinetic and physical properties similar to the purified rat liver enzyme. The efficient expression of this low abundance hepatic protein in bacteria provides a system for in vitro analysis of mutations of the enzyme.

AB - Rat Liver glucokinase was expressed in Escherichia coli by using an expression system based on bacteriophage T7 RNA polymerase. The expressed protein starts with the predicted initiator methionine residue and ends at the appropriate carboxyl terminal residue. It was partially purified by ammonium sulfate precipitation and gel filtration and had kinetic and physical properties similar to the purified rat liver enzyme. The efficient expression of this low abundance hepatic protein in bacteria provides a system for in vitro analysis of mutations of the enzyme.

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SN - 0006-291X

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JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

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ER -

Expression of rat hepatic glucokinase in Escherichia coli

Abstract

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