Rapid purification of recombinant human lipocortin-I secreted from Saccharomyces cerevisiae

Cited 0 time in scopus
Metadata Downloads
Title
Rapid purification of recombinant human lipocortin-I secreted from Saccharomyces cerevisiae
Author(s)
Bong Hyun Chung; Soo Wan Nam
Bibliographic Citation
Biotechnology and Bioprocess Engineering, vol. 5, pp. 242-246
Publication Year
2000
Abstract
Human lipocortin-I was expressed as a secretory product by Saccharomyces cerevisiae harboring an expression system consisting of GAL10 promoter, inulinase signal sequence and lipocortin-I terminator. Fed-batch fermentation was carried out to overproduce recombinant human lipocortin-I. The culture medium was desalted and concentrated by ultrafiltration, and then subjected to hydroxyapatite column chromatography. The lipocortin-I was purified to >98% purity by single-step hydroxyapatite column chromatography. However, it was found that the purified lipocortin-I was a proteolytically-cleaved form which was cleaved immediately after the basic amino acid Lys26.
Keyword
human lipocortin-ISaccharomyces cerevisiaesecretory producthydroxyapatite column chromatography
ISSN
1226-8372
Publisher
Springer
DOI
http://dx.doi.org/10.1007/BF02942180
Type
Article
Appears in Collections:
1. Journal Articles > Journal Articles
Files in This Item:
  • There are no files associated with this item.


Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.