Structural and functional characterization of the abnormal Z alpha 1-antitrypsin isolated from human liver.
alpha 1-Antitrypsin has been isolated from liver inclusion bodies of a subject with a homozygous Z deficiency. The inhibitor was recovered in a fully active form by extraction in high salt at either pH 2.0 or pH 8.0. Carbohydrate analysis indicated a protein in the 'high mannose' form, and this was collaborated by its sensitivity to endo-beta N-glucosaminidase. These data suggest that the abnormal alpha 1-antitrypsin is blocked in the secretory pathway prior to its entrance into the Golgi, and that this blockage is not due to a gross misfolding of the polypeptide.
D002241:Carbohydrates / Q000032:analysis; D006720:Homozygote; D006801:Humans; D008099:Liver / Q000378:metabolism*; D008970:Molecular Weight; D009154:Mutation; D010641:Phenotype; D000515:alpha 1-Antitrypsin / Q000235:genetics* / Q000302:isolation & purification
D002241:Carbohydrates; C043392:SERPINA1 protein, human; D000515:alpha 1-Antitrypsin