| Popis: |
Three soluble invertase (EC 3.2.1.26) isoforms from Easter lily (Lilium longiflorum Thunb. cv. Nellie White) flower buds were purified to apparent homogeneity. Non-denaturing PAGE showed one band for all three invertases that corresponded to the invertase activity. SDS-PAGE of purified invertase I gave a single band at 78 kDa, whereas invertases II and III gave three bands at 54, 52 and 24 kDa. Antibodies against tomato fruit acid invertase and Urtica dioica leaf acid invertase recognized all three invertase isoforms, whereas antibodies against wheat coleoptile acid invertase recognized only 56- and 54-kDa bands of invertases II and III. Antibodies against wheat coleoptile invertase recognized the 54- and 52-kDa proteins from crude extracts of all flower organs, and a 72-kDa protein in both leaf and bulb scale extracts. All three invertases bound to Con-A peroxidase. Deglycosylation of invertase I with glycopeptidase F was complete and resulted in a peptide of 75 kDa. Invertases II and III were deglycosylated partially by glycopeptidase F and resulted in proteins of 53, 51, 50 and 22 kDa. Invertase I was localized only in anther and filament, whereas the other two isoforms were present in all flower organs. |
Plný text