Disruption of the Lys‐290‐Glu‐342 salt bridge in human α1‐antitrypsin does not prevent its synthesis and secretion

FEBS Letters

Foreman, R.C.¹ 

[1] Department of Pharmaceutical Chemistry, The School of Pharmacy, University of London, 29/39 Brunswick Square, London WC1N 1AX, England

关键词: α1-Antitrypsin;    Z variant;    Site-directed mutagenesis;    α-Antitrypsin secretion;    (Xenopus oocyte);   

DOI  :  10.1016/0014-5793(87)80760-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The object of this work was to test the hypothesis that failure to secrete the Z variant of human α₁-antitrypsin is related to the loss of a particular structural feature, the Lys-290 to Glu-342 salt bridge. Oligonucleotide-directed mutagenesis was used to disrupt the salt bridge by substituting a glutamic acid for lysine at residue 290. RNA transcripts prepared from this mutant DNA and from the normal cDNA were both able to direct the synthesis of protein in a cell-free system and after injection into Xenopus oocytes. Furthermore, the constructed mutant α-antitrypsin was secreted as readily as the normal inhibitor.

【 授权许可】

Unknown