Characterization of endopolygalacturonase (EC 3.2.1.15) from Aspergillus niger as glycoprotein by electrophoretic methods and lectin affino‐blotting

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Abstract
Chromatographically purified endopolygalacturonase (PG) from Aspergillus niger was deglycosylated with N‐glycosidase F (PNGase F) and characterized by means of sodium dodecyl sulfate (SDS)‐electrophoresis, polyacrylamide gel electrophoresis (PAGE) without denaturing agents, isoelectric focusing (IEF) and lectin affino‐blotting. The results show that PG, which is apparently homogeneous in SDS‐PAGE but heterogeneous in IEF and PAGE, consists of at least two polypeptide chains with different glycosylation patterns. The component with the higher electrophoretic mobility is deglycosylated with PNGase F and reacts with concanavalin A (Con A) and Galanthus nivalis agglutinin (GNA), indicating a “high mannose” or “hybrid”‐type of glycoprotein (GP). The other component may contain O‐glycosidically linked mannose, N‐acetylglucosamine or glucose.

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