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Title 

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

Authors 

Bong Hyun ChungSoo Wan Nam

Publisher 

Springer Verlag (Germany)

Issue Date 

2000

Citation 

Biotechnology and Bioprocess Engineering, vol. 5, no. 0, pp. 242-246

Keywords 

human lipocortin-ISaccharomyces cerevisiaesecretory producthydroxyapatite column chromatography

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.

ISSN 

1226-8372

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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