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Translation and processing of normal (PiMM) and abnormal (PiZZ) human α 1 ‐antitrypsin
Author(s) -
Bathurst I.C.,
Stenflo J.,
Errington D.M.,
Carrell R.W.
Publication year - 1983
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(83)80622-x
Subject(s) - alpha 1 antitrypsin deficiency , translation (biology) , biology , genetics , computational biology , immunology , gene , messenger rna
Human liver mRNA isolated from subjects phenotyped as homozygous PiMM or PiZZ α 1 ‐antitrypsin, was translated in a reticulocyte cell‐free system, and α 1 ‐antitrypsin identified by immunoprecipitation. In the presence of dog pancreas membranes the translated α 1 ‐antitrypsin appeared as a larger product. Treatment with endo‐β‐ N ‐glucosaminidase yielded a protein smaller than the reticulocyte translated product, presumably due to removal of the N‐terminal signal sequence by membranes and sugar residues by endo‐β‐ N ‐glucosaminidase. Quantitation of α 1 ‐antitrypsin translated from PiMM and PiZZ livers suggests that both mRNA species were present at the same cellular concentration, and that processing to the core glycosylation stage proceeded at identical rates.