Purification and characterization of α₁-antitrypsin secreted by recombinant yeast Saccharomyces diastaticus

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Title
Purification and characterization of α₁-antitrypsin secreted by recombinant yeast Saccharomyces diastaticus
Author(s)
Ki Sun Kwon; Mooyoung Song; Myeong Hee Yu
Bibliographic Citation
Journal of Biotechnology, vol. 42, pp. 191-195
Publication Year
1995
Abstract
The secreted human α1-antitrypsin (α1AT) produced by yeast was purified from the culture medium by ultrafiltration, ammonium sulfate fractionation (60-75% saturation), protamine sulfate treatment, and ion-exchange chromatography. Molecular mass of the purified α1AT was 52 kDa, which is similar to that of human plasma α1AT. Yeast-produced α1AT was fully functional as an inhibitor compared with the plasma form. Unlike plasma (α1AT, however, treatment of the yeast-produced α1AT with endoglycosidase H decreased the molecular mass to that of recombinant α1AT produced in Escherichia coli, indicating the high-mannose type N-linked glycosylation of the secreted α1AT. Glycosylation in yeast cells enhanced kinetic stability of α1AT towards heat deactivation.
Keyword
α1-Antitrypsinglycosylationstability
ISSN
0168-1656
Publisher
Elsevier
DOI
http://dx.doi.org/10.1016/0168-1656(95)00079-6
Type
Article
Appears in Collections:
Aging Convergence Research Center > 1. Journal Articles
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