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KMID : 1094720000050040242
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Biotechnology and Bioprocess Engineering
2000 Volume.5 No. 4 p.242 ~ p.246
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Rapid purification of recombinant human lipocortin-I secreted from Saccharomyces cerevisiae
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Chung Bong-Hyun
Nam Soo-Wan
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Abstract
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Human lipocortin-I was expressed as a secretory product bySaccharomyces cerevisiae harboring an expression system consisting ofGAL10 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.
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KEYWORD
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human lipocortin-I, Saccharomyces cerevisiae, secretory product, hydroxyapatite column chromatography
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