Olczak M, Watorek W
Institute of Biochemistry and Molecular Biology, Wrocław University, Poland.
Arch Biochem Biophys. 1998 Dec 1;360(1):85-92. doi: 10.1006/abbi.1998.0927.
Peptide mapping of lupin acid phosphatase clearly demonstrated the homology between its two subunits. Sequenced tryptic peptides also showed 78% identity (92% similarity) to the red bean acid phosphatase. Peptides exclusive for the 50-kDa subunit are homologous to N-terminally located sequences in red bean acid phosphatase, leading to the assumption that the shorter subunit of lupin acid phosphatase is generated by the deletion of the N-terminal part of the longer subunit. Carbohydrate moiety was found to be identical in both subunits. Oligosaccharide chains released by hydrazinolysis from the both subunits were fluorescently labeled and separated by HPLC. The structure of oligosaccharides was elucidated by exoglycosidase sequencing. Seventeen percent of isolated glycans were found to be of the high-mannose type, while the rest belonged to plant complex-type structures. Most of the complex glycans were fucosylated and xylosylated; some were fucosylated or xylosylated only.
