Molecular properties of recombinant human alpha1-antitrypsin produced in Escherichia coli and in vitro translation system

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Title
Molecular properties of recombinant human alpha1-antitrypsin produced in Escherichia coli and in vitro translation system
Author(s)
Kee Nyung Lee; Hwa Soo Shin; Ki Sun Kwon; Sang Dai Park; Myeong Hee Yu
Bibliographic Citation
Molecules and Cells, vol. 3, no. 1, pp. 71-74
Publication Year
1993
Abstract
The cDNA encoding human al-antitrypsin (alAT) was expressed in Escherichia coli upto ?40% of total cellular proteins. The recombinant alAT carrying the Z type mutation (Glu342?>Lys) were accumulated as aggregates inside the E. coli cells while the wild type alAT were produced as a soluble form. The aggregation caused by the Z mutation became more significant as the growth temperature increased from 30 t to 37 t. A protein folding assay of alAT on SDS-polyaciylamide gel electrophoresis revealed that the Z polypeptides translated in vitro were in a conformation which could not bind elastase but rather served as a substrate for the protease. The results are consistent with the previously known Z type defects, aggregation inside the hepatocytes of patients and temperature-dependent oli-’ gomerization of the purified Z protein, ^rhe E. coli expression system and the folding (assay of in vitro translation product develoj)ed in the present study may be further explored / for characterization of other genetic variants of alAT.
ISSN
1016-8478
Publisher
Korea Soc-Assoc-Inst
Type
Article
Appears in Collections:
Aging Convergence Research Center > 1. Journal Articles
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