Characterization of isoforms of pectin methylesterase of Linum usitatissimum using polyclonal antibodies
1995
Mareck, A. (Equipe Parois et Polymeres Parietaux (France)) | Gaffe, J. | Morvan, O. | Alexandre, C. | Morvan, C.
In flax (Linum usitatissimum, c.v. Ariane) pectin methylesterase (PME) (EC 3.1.1.11), ionically bound to cell-wall, was composed mainly of forms with isoelectric points (pIs) of 7.1, 7.6 and 9.6. Minor forms, with acid pIs (4.5, 4.8 and 6.3), were detected during the purification of two of these forms. Polyclonal antibodies were raised against the isoenzymes presenting pIs of 7.1 and 7.6. Antibodies recognized antigenic forms and two close proteins in the basic range which could be associated to the PME activity with pI of 9.6. Antibodies did not recognize any acid forms and exhibited no cross-reactivity with proteins resolved in the cellular content. Antigenicity was related mainly to the protein part of the glycosylated enzyme. The antibodies against flax PME did not cross-react with PMEs from Citrus and tomato and with glycosylated proteins of various sources. Specificity of anti-PME antibodies was judged sufficient to localize the recognized forms on tissue prints of flax hypocotyls. Although PME was distributed in the whole parts of hypocotyl, staining was not homogeneous and appeared reinforced in the apical zone. In the basal part, epidermis was more contrasted than internal tissues
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