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Expression of a deleted variant of human plasminogen in Escherichia coli

Expression of a deleted variant of human plasminogen in Escherichia coli A recombinant plasmid carrying a modified gene of human plasminogen (mini-plasminogen), lacking four kringle domains and an amino terminal fragment, and containing an additional oligopeptide of six N-terminal histidine residues has been constructed. The plasmid was used for transformation of E. coli JM 109 cells to obtain a strain producing a recombinant modified human plasminogen. The target protein is superexpressed in a form of inclusion bodies and is composed of more than 50% insoluble protein. The renaturated and chromatographically purified protein exhibits amidolytic activity specific for plasminogen proenzyme in a fibrinolytic system. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Applied Biochemistry and Microbiology Springer Journals

Expression of a deleted variant of human plasminogen in Escherichia coli

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References (18)

Publisher
Springer Journals
Copyright
Copyright © 2010 by Pleiades Publishing, Ltd.
Subject
Life Sciences; Medical Microbiology ; Microbiology ; Biochemistry, general
ISSN
0003-6838
eISSN
1608-3024
DOI
10.1134/S0003683810080077
Publisher site
See Article on Publisher Site

Abstract

A recombinant plasmid carrying a modified gene of human plasminogen (mini-plasminogen), lacking four kringle domains and an amino terminal fragment, and containing an additional oligopeptide of six N-terminal histidine residues has been constructed. The plasmid was used for transformation of E. coli JM 109 cells to obtain a strain producing a recombinant modified human plasminogen. The target protein is superexpressed in a form of inclusion bodies and is composed of more than 50% insoluble protein. The renaturated and chromatographically purified protein exhibits amidolytic activity specific for plasminogen proenzyme in a fibrinolytic system.

Journal

Applied Biochemistry and MicrobiologySpringer Journals

Published: Nov 14, 2010

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