Circulating proalbumin associated with a second case of antitrypsin Pittsburgh.
We report here the conclusive identification of circulating proalbumin of normal N-terminal sequence (Arg Gly Val Phe Arg Arg Asp Ala) in a second child with the alpha 1-antitrypsin Pittsburgh 358 Met-->Arg mutation. As in the first case, the proalbumin made up 3-5% of the total serum albumin. The finding of proalbumin associated with a second de novo mutation at the inhibitory site bait of antitrypsin confirms our earlier hypothesis; that antitrypsin Pittsburgh was acting as a specific intracellular inhibitor of the hepatic proalbumin convertase and that antitrypsin Pittsburgh could be used as a probe to identify the proprotein convertase.
Brennan
S O
SO
Molecular Pathology Laboratory, Christchurch Hospital, New Zealand.
Sheat
J M
JM
Aiach
M
M
D000595:Amino Acid Sequence; D002648:Child; D003166:Complement Activating Enzymes / Q000037:antagonists & inhibitors; D006801:Humans; D008099:Liver / Q000201:enzymology; D008969:Molecular Sequence Data; D011228:Prealbumin / Q000032:analysis* / Q000302:isolation & purification; D000515:alpha 1-Antitrypsin / Q000032:analysis*
D011228:Prealbumin; D000515:alpha 1-Antitrypsin; C038915:alpha 1-antitrypsin Pittsburgh; D003166:Complement Activating Enzymes