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The effect of amino acid substitutions at position 342 on the secretion of human α 1 ‐antitrypsin from Xenopus oocytes
Author(s) -
Wu Ying,
Foreman R.C.
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80962-i
Subject(s) - xenopus , secretion , chemistry , amino acid , position (finance) , microbiology and biotechnology , biochemistry , biology , gene , finance , economics
A glutamic acid to lysine change in the Z variant of human α 1 ‐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 α 1 ‐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.