Processing of N-glycans of two yellow lupin phosphohydrolases during seed maturation and dormancy.
Acid phosphatase (AP) and diphosphonucleoside phosphatase/phosphodiesterase (PPD1) were purified from yellow lupin (Lupinus luteus L.) immature green seeds (40 days after blooming), dry seeds (40 days later) and dry seeds stored for 160 days. Both enzymes are known to differ in the type of N-glycosylation: the first has an N-glycosylation pattern typical for a vacuolar protein, while the second enzyme has a pattern typical for an extracellular or membrane-bound protein. N-Glycans were released from each of the enzyme preparations, fluorescence labeled, separated and identified by HPLC (GlycoSep N and GlycoSep H columns). Changes in the level of each N-glycan during seed maturation and dormancy were compared. The results show that N-glycan processing in the case of AP and PPD1-two proteins residing in the same plant organ, but possibly in different compartments-is not synchronized and performed not only in metabolically active maturing seeds, but also in metabolically inactive dormant seeds.
Olczak
Mariusz
M
Wroclaw University, Institute of Biochemistry and Molecular Biology, Tamka 2, Poland.
Watorek
Wieslaw
W
D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D007887:Fabaceae / Q000196:embryology*; D006868:Hydrolysis; D008969:Molecular Sequence Data; D010744:Phosphoric Monoester Hydrolases / Q000302:isolation & purification / Q000378:metabolism*; D011134:Polysaccharides / Q000737:chemistry / Q000378:metabolism*; D012639:Seeds / Q000201:enzymology / Q000254:growth & development / Q000378:metabolism*; D013050:Spectrometry, Fluorescence
D011134:Polysaccharides; D010744:Phosphoric Monoester Hydrolases