Overproduction, secretion, isolation and properties of recombinant alkaline phosphatase encoded in Escherichia coli

M. A. Nesmeyanova; A. E. Kalinin; A. L. Karamyshev; N. I. Mikhaleva; V. I. Krupyanko

doi:10.1016/S0032-9592(97)87450-X

Overproduction, secretion, isolation and properties of recombinant alkaline phosphatase encoded in Escherichia coli

M. A. Nesmeyanova, A. E. Kalinin, A. L. Karamyshev, N. I. Mikhaleva, V. I. Krupyanko

Physiology

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10 Scopus citations

Abstract

Expression of the phoA gene cloned in a multicopy plasmid in Escherichia coli E15 (ΔphoA) results in overproduction of the alkaline phosphatase. Secretion occurs into the periplasm and the culture medium, and accumulation of a precursor (prePhoA) occurs as insoluble aggregates. All these forms of the enzyme were purified and their properties were studied. Extracellular and periplasmic enzymes differ in V(max) and K(m) values but have similar activation energies (E(a)). Mature alkaline phosphatase and intermediate forms can be isolated from one E. coli culture.

Original language	English (US)
Pages (from-to)	1-7
Number of pages	7
Journal	Process Biochemistry
Volume	32
Issue number	1
DOIs	https://doi.org/10.1016/S0032-9592(97)87450-X
State	Published - Jan 1997

ASJC Scopus subject areas

Bioengineering
Biochemistry
Applied Microbiology and Biotechnology

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abstract = "Expression of the phoA gene cloned in a multicopy plasmid in Escherichia coli E15 (ΔphoA) results in overproduction of the alkaline phosphatase. Secretion occurs into the periplasm and the culture medium, and accumulation of a precursor (prePhoA) occurs as insoluble aggregates. All these forms of the enzyme were purified and their properties were studied. Extracellular and periplasmic enzymes differ in V(max) and K(m) values but have similar activation energies (E(a)). Mature alkaline phosphatase and intermediate forms can be isolated from one E. coli culture.",

author = "Nesmeyanova, {M. A.} and Kalinin, {A. E.} and Karamyshev, {A. L.} and Mikhaleva, {N. I.} and Krupyanko, {V. I.}",

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AU - Nesmeyanova, M. A.

AU - Kalinin, A. E.

AU - Karamyshev, A. L.

AU - Mikhaleva, N. I.

AU - Krupyanko, V. I.

PY - 1997/1

Y1 - 1997/1

N2 - Expression of the phoA gene cloned in a multicopy plasmid in Escherichia coli E15 (ΔphoA) results in overproduction of the alkaline phosphatase. Secretion occurs into the periplasm and the culture medium, and accumulation of a precursor (prePhoA) occurs as insoluble aggregates. All these forms of the enzyme were purified and their properties were studied. Extracellular and periplasmic enzymes differ in V(max) and K(m) values but have similar activation energies (E(a)). Mature alkaline phosphatase and intermediate forms can be isolated from one E. coli culture.

AB - Expression of the phoA gene cloned in a multicopy plasmid in Escherichia coli E15 (ΔphoA) results in overproduction of the alkaline phosphatase. Secretion occurs into the periplasm and the culture medium, and accumulation of a precursor (prePhoA) occurs as insoluble aggregates. All these forms of the enzyme were purified and their properties were studied. Extracellular and periplasmic enzymes differ in V(max) and K(m) values but have similar activation energies (E(a)). Mature alkaline phosphatase and intermediate forms can be isolated from one E. coli culture.

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Overproduction, secretion, isolation and properties of recombinant alkaline phosphatase encoded in Escherichia coli

Abstract

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