High-level production and isolation of human recombinant alpha 1-proteinase inhibitor in yeast.

Abstract:

:The cDNA coding for mature human alpha 1-proteinase inhibitor (alpha 1-PI) has been inserted into a variety of yeast expression vectors. Yeast cells transformed with these plasmids were then assayed for the production of mature, unglycosylated alpha 1-PI. The production level is optimal when the recombinant plasmid carries the TDH promoter, the complete 2mu and the leu2D selection marker. Biologically active recombinant alpha 1-PI can be purified either analytically, by affinity chromatography using a monoclonal antibody, or on a large scale, by a procedure involving precipitation of high-Mr yeast material with polyethylene glycol 3300 followed by successive chromatography on DEAE-agarose, Zn-chelate agarose, kappa-chain agarose, heparin-agarose and aminohexyl-agarose.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Hoylaerts M,Weyens A,Bollen A,Harford N,Cabezón T

doi

10.1016/0014-5793(86)81391-6

subject

Has Abstract

pub_date

1986-08-11 00:00:00

pages

83-7

issue

1

eissn

0014-5793

issn

1873-3468

pii

0014-5793(86)81391-6

journal_volume

204

pub_type

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