Production of Drosophila melanogaster acetylcholinesterase in Saccharomyces cerevisiae

K. C.A. Stopps; B. P.G. Curran; S. A. Khalawan; C. A. Malcolm

doi:10.1023/A:1010330015598

Production of Drosophila melanogaster acetylcholinesterase in Saccharomyces cerevisiae

K. C.A. Stopps
, B. P.G. Curran
, S. A. Khalawan
, C. A. Malcolm

Research output: Contribution to journal › Article › peer-review

Abstract

Biologically active acetylcholinesterase from Drosophila melanogaster was constitutively expressed from a high copy number plasmid in Saccharomyces cerevisiae. Cellular metabolism and plasmid copy number were unaffected by expression. Based on comparative PMSF inhibition, the K_cat value (6430 mol s^-1) was commensurate with human and Torpedo acetylcholinesterases. A 1.7 knt truncated mRNA transcript was observed on Northern blot analysis.

Original language	English
Pages (from-to)	417-422
Number of pages	6
Journal	Biotechnology Letters
Volume	23
Issue number	6
DOIs	https://doi.org/10.1023/A:1010330015598
Publication status	Published - 1 Mar 2001

Keywords

Acetylcholinesterase
Drosophila melanogaster
Saccharomyces cerevisiae

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10.1023/A:1010330015598

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title = "Production of Drosophila melanogaster acetylcholinesterase in Saccharomyces cerevisiae",

abstract = "Biologically active acetylcholinesterase from Drosophila melanogaster was constitutively expressed from a high copy number plasmid in Saccharomyces cerevisiae. Cellular metabolism and plasmid copy number were unaffected by expression. Based on comparative PMSF inhibition, the Kcat value (6430 mol s-1) was commensurate with human and Torpedo acetylcholinesterases. A 1.7 knt truncated mRNA transcript was observed on Northern blot analysis.",

keywords = "Acetylcholinesterase, Drosophila melanogaster, Saccharomyces cerevisiae",

author = "Stopps, \{K. C.A.\} and Curran, \{B. P.G.\} and Khalawan, \{S. A.\} and Malcolm, \{C. A.\}",

note = "Funding Information: We thank Dr V. Bugeja for the densitometry carried out at the University of Hertfordshire. This work was supported by a grant to C.A. Malcolm and B.P.G. Curran from the Wellcome Trust (No. 034732/Z/91/Z).",

year = "2001",

month = mar,

day = "1",

doi = "10.1023/A:1010330015598",

language = "English",

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pages = "417--422",

journal = "Biotechnology Letters",

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T1 - Production of Drosophila melanogaster acetylcholinesterase in Saccharomyces cerevisiae

AU - Stopps, K. C.A.

AU - Curran, B. P.G.

AU - Khalawan, S. A.

AU - Malcolm, C. A.

N1 - Funding Information: We thank Dr V. Bugeja for the densitometry carried out at the University of Hertfordshire. This work was supported by a grant to C.A. Malcolm and B.P.G. Curran from the Wellcome Trust (No. 034732/Z/91/Z).

PY - 2001/3/1

Y1 - 2001/3/1

N2 - Biologically active acetylcholinesterase from Drosophila melanogaster was constitutively expressed from a high copy number plasmid in Saccharomyces cerevisiae. Cellular metabolism and plasmid copy number were unaffected by expression. Based on comparative PMSF inhibition, the Kcat value (6430 mol s-1) was commensurate with human and Torpedo acetylcholinesterases. A 1.7 knt truncated mRNA transcript was observed on Northern blot analysis.

AB - Biologically active acetylcholinesterase from Drosophila melanogaster was constitutively expressed from a high copy number plasmid in Saccharomyces cerevisiae. Cellular metabolism and plasmid copy number were unaffected by expression. Based on comparative PMSF inhibition, the Kcat value (6430 mol s-1) was commensurate with human and Torpedo acetylcholinesterases. A 1.7 knt truncated mRNA transcript was observed on Northern blot analysis.

KW - Acetylcholinesterase

KW - Drosophila melanogaster

KW - Saccharomyces cerevisiae

UR - https://www.scopus.com/pages/publications/0035057304

U2 - 10.1023/A:1010330015598

DO - 10.1023/A:1010330015598

M3 - Article

AN - SCOPUS:0035057304

SN - 0141-5492

VL - 23

SP - 417

EP - 422

JO - Biotechnology Letters

JF - Biotechnology Letters

IS - 6

ER -

Production of Drosophila melanogaster acetylcholinesterase in Saccharomyces cerevisiae

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