PURIFICATION AND PARTIAL CHARACTERIZATION OF... : New England Journal of Medicine (original) (raw)

PURIFICATION AND PARTIAL CHARACTERIZATION OF PAS-POSITIVE INCLUSION BODIES FROM THE LIVER IN ALPHA1-ANTITRYPSIN DEFICIENCY

• Sten Eriksson
• Christer Larsson

New England Journal of Medicine

292

(

4

)

:p

176

-

180

,

January 23, 1975

.

| DOI: 10.1056/NEJM197501232920403

Abstract

To characterize the periodic acid-Schiff-positive inclusion bodies from cirrhotic livers of patients with homozygous alpha1-antitrypsin deficiency we isolated and analyzed such material. The main component of the inclusion bodies was a protein with approximately the same molecular size as serum alpha1-antitrypsin. Immunologic similarity between the isolated protein and serum alpha1-antitrypsin was established by the isolate's ability to react with fluorescein-isothiocyanate-conjugated antibodies against serum alpha1-antitrypsin and to raise antibodies against it in rabbits, and with the double immunodiffusion technic.

On agarose-gel electrophoresis hepatic antitrypsin migrated as an alpha2-globulin before and after neuraminidase treatment. Chemical analysis showed a complete absence of sialic acid. Hepatic antitrypsin had a pronounced tendency to form insoluble macroaggregates.

An insufficient sialylation of antitrypsin in the liver appears to be one of the basic defects in alpha1-antitrypsin deficiency. (N Engl J Med 292:176-180, 1975)

Copyright © Owned, published, and © copyrighted, 1975, by the MASSACHUSETTS MEDICAL SOCIETY