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Title 

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

Authors 

Ki Sun KwonMooyoung SongMyeong Hee Yu

Publisher 

Elsevier

Issue Date 

1995

Citation 

Journal of Biotechnology, vol. 42, no. 0, pp. 191-195

Keywords 

α1-Antitrypsinglycosylationstabilityalpha 1 antitrypsinprotein purificationsaccharomyces cerevisiaealpha 1-antitrypsinrecombinant proteinssaccharomycessaccharomyces cerevisiae var. diastaticus

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.

ISSN 

0168-1656

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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