A STUDY ON GLYCOSYLATION OF CATIONIC PEANUT PEROXIDASE

Cationic peroxidase from a cell suspension culture has two heterogeneously glycosylated forms, based on their Concanavalin A column binding property, namely CP- and CP+. In these two forms three out of five potential glycosylation sites are used. Asn60 and Asn185 are located in hydrophilic β-turns, while Asn144 in a hydrophobic β-sheet. Asn209 and Asn275 lacking glycans all have a proline residue at the C-terminal of the consensus sequence. The difference between CP- and CP+ is due to the heterogeneous glycosylation at individual glycosylation sites. © 1993 Academic Press, Inc.