1993
DOI: 10.1007/bf00749938
|View full text |Cite
|
Sign up to set email alerts
|

Abstract: Production of recombinant human acetylcholinesterase (AChE) by a high producer human embryonic kidney cell line (293) was evaluated by three main cell propagation systems; surface propagator, fixed-bed reactor and stirred microcarrier cultures. The recombinant cell line expresses AChE levels as high as 10-20 mg/l/day. System productivities in either the surface propagator (multitray system), or in the fixed-bed reactor (polyurethane macroporous sponges) were 4-8 mg AChE/l/day during a production period of 8 da… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
4
1

Citation Types

1
13
0

Year Published

1993
1993
2013
2013

Publication Types

Select...
5
2
1

Relationship

0
8

Authors

Journals

citations
Cited by 19 publications
(14 citation statements)
references
References 25 publications
1
13
0
Order By: Relevance
“…Stable recombinant cell clones expressing high levels of each of the mutants were established according to the procedure described previously [20]. The resulting recombinant clones were propagated in multitray systems [21 ]. The secreted enzymes in the cell supernatant (2-6 liters) were purified (over 90% purity) by affinity chromatography as described previously [20].…”
Section: Recombinant Hua Che and Its Mutantsmentioning
confidence: 99%
“…Stable recombinant cell clones expressing high levels of each of the mutants were established according to the procedure described previously [20]. The resulting recombinant clones were propagated in multitray systems [21 ]. The secreted enzymes in the cell supernatant (2-6 liters) were purified (over 90% purity) by affinity chromatography as described previously [20].…”
Section: Recombinant Hua Che and Its Mutantsmentioning
confidence: 99%
“…Indeed the successful exploitation of the scavenging potential of administered cholinesterase has been demonstrated in rodents and in non-human primates [1][2][3][4][5]. The use of human AChE (HuAChE) as an efficient bioscavenger has been advanced by the development of recombinant production systems [6][7][8], and the introduction of catalytically favourable mutations [9][10][11][12]. Yet, the short circulatory residence time of the various recombinant AChE preparations [13][14][15][16] represents one of the factors that precludes the development of an efficient AChE-based recombinant bioscavenger, and the formulation of a method for the pharmacokinetic improvement of the enzyme is a major biotechnological challenge.…”
Section: Introductionmentioning
confidence: 99%
“…Expression of the human [15,16], mouse [17,18] and rat [19] AChEs in recombinant systems allowed for a thorough analysis of the architecture as well as the catalytic function of the enzymes. Furthermore, the ability to generate large quantities of human recombinant enzyme in human embryonal kidney 293 cells (HEK-293) [20], together with mutagenesis studies dissecting the interactions of this enzyme with its various ligands [21][22][23][24][25][26], has set a basis for the use of human AChE (HuAChE) as a therapeutic agent in organophosphorus poisoning. However, the use of recombinant HuAChE (rHuAChE) as a biological scavenger is complicated by its rapid clearance from the circulation [27].…”
Section: Introductionmentioning
confidence: 99%