The effect of amino acid substitutions at position 342 on the secretion of human α1‐antitrypsin from Xenopus oocytes
- 30 July 1990
- journal article
- Published by Wiley in FEBS Letters
- Vol. 268 (1) , 21-23
- https://doi.org/10.1016/0014-5793(90)80962-i
Abstract
A glutamic acid to lysine change in the Z variant of human α1-antitrypsin is associated with a failure to secrete the protein from synthesising cells. The block in export of the protein may be caused either by the loss of an acidic residue or the introduction of a basic one at this point in the polypeptide chain. Site-directed mutagenesis has been used to construct novel α1-antitrypsin mutants which show that the side chain interactions from Glu-342 are not obligatory for protein export and it is rather the introduction of a basic residue at this point which produces the intracellular accumulation of the protein.Keywords
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