Enhanced expression of human prostaglandin H synthase-2 in the yeast Pichia pastoris and removal of the C-terminal tag with bovine carboxypeptidase A
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- 作者：Kaia Kukk ; Nigulas Samel ; nigulas.samel@ttu.ee" class="auth_mail" title="E-mail the corresponding author
- 关键词：AA ; arachidonic acid ; AOX1 ; alcohol oxidase 1 ; boCPA ; bovine carboxypeptidase A ; CT ; threshold cycle ; GAP ; glyceraldehyde 3-phosphate dehydrogenase ; h ; human ; HIS4 ; histidinol dehydrogenase ; qPCR ; quantitative PCR ; PGHS ; prostaglandin H synthase ; WCW ; wet cell weight
- 刊名：Journal of Biotechnology
- 出版年：2016
- 出版时间：10 August 2016
- 年：2016
- 卷：231
- 期：Complete
- 页码：224-231
- 全文大小：755 K
文摘
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Octa-histidine tagged hPGHS-2 was expressed in the yeast Pichia pastoris.
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Compared to constitutive expression, methanol-induced expression yielded more hPGHS-2.
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Bovine carboxypeptidase A was used to elute hPGHS-2 from the Ni-affinity resin.
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3 mg of pure de-tagged hPGHS-2 was obtained from 1 l of P. pastoris culture.