title: The serum sialyltransferase activity in alpha 1-antitrypsin deficiency.
abstract: alpha 1-Antitrypsin phenotypes Pi M and Z, purified by the thiol-disulfide exchange procedure, were desialylated by treatment with neuraminidase covalently coupled to Sepharose and used as acceptors of sialic acid in an assay system for serum sialic acid transferase (CMP-N-acetylneuraminate:D-galactosyl-glycoprotein N-acetylneuraminyltransferase, EC 2.4.99.1) activity. Both asialoantitrypsins were equally effective as acceptors in contrast to native Pi Z antitrypsin which did not accept any sialic acid. Serum sialyltransferase activity was determined in 38 adult alpha 1-antitrypsin deficient individuals (Pi Z, MZ, FZ, SZ) with normal liver function and was found to be of the same magnitude as the activity in normal individuals (Pi M). Equal activities were also found in 5 Pi Z patients with cirrhosis of the liver. The results strongly argue against the concept that sialyltransferase deficiency provides the molecular basis for alpha 1-antitrypsin deficiency.
mesh_terms: D005215:Fasting; D005260:Female; D006801:Humans; D008103:Liver Cirrhosis / Q000201:enzymology; D008297:Male; D010641:Phenotype; D012794:Sialic Acids / Q000378:metabolism; D012799:Sialyltransferases / Q000097:blood*; D014166:Transferases / Q000097:blood*; D000515:alpha 1-Antitrypsin / Q000302:isolation & purification; D019896:alpha 1-Antitrypsin Deficiency
chemical_list: D012794:Sialic Acids; D000515:alpha 1-Antitrypsin; D014166:Transferases; D012799:Sialyltransferases