Structural study of the sugar chains of alpha-amylases produced ectopically in tumors.
About thirty percent of two alpha-amylases produced from a serous papillary cystadenocarcinoma of the ovarium (case 1) and a bronchioloalveolar adenocarcinoma of the lung (case 2) was glycoproteins containing 1 mol of asparagine-linked sugar chain, respectively. The structures of the sugar moieties were found by sequential enzymatic degradation and methylation analysis to be as follows: [(Gal beta 1 leads to 4)0 or 1GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3)][GlcNAc beta 1 leads to 2Man alpha 1 leads to 3(6)]Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and [(Gal beta 1 leads to 4)0 or 1GlcNAc beta 1 leads to 2Man alpha 1 leads to 6][NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3]Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc. Structures of asparagine-linked sugar chains were the same in the tumors of cases 1 and 2 and were incomplete in comparison with those of the parotid amylase.
D000230:Adenocarcinoma / Q000201:enzymology*; D000681:Amylases / Q000302:isolation & purification*; D002241:Carbohydrates / Q000302:isolation & purification*; D055598:Chemical Phenomena; D002621:Chemistry; D003536:Cystadenocarcinoma / Q000201:enzymology*; D005260:Female; D006801:Humans; D008175:Lung Neoplasms / Q000201:enzymology*; D010051:Ovarian Neoplasms / Q000201:enzymology*; D000516:alpha-Amylases / Q000302:isolation & purification*
D002241:Carbohydrates; D000681:Amylases; D000516:alpha-Amylases