Related Experiment Videos
A study on glycosylation of cationic peanut peroxidase
1Department of Plant Sciences, University of Western Ontario, London, Canada.
Biochemical and Biophysical Research Communications
|August 16, 1993
Abstract:
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 beta-turns, while Asn144 in a hydrophobic beta-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.