CHARACTERIZATION OF COMMON CARBOHYDRATE ANTIGENIC DETERMINANTS ON SOYA BEAN CELL-WALL ENZYMES

Citation
M. Teissere et al., CHARACTERIZATION OF COMMON CARBOHYDRATE ANTIGENIC DETERMINANTS ON SOYA BEAN CELL-WALL ENZYMES, Plant and Cell Physiology, 35(1), 1994, pp. 121-125
Citations number
20
Categorie Soggetti
Plant Sciences
Journal title
ISSN journal
00320781
Volume
35
Issue
1
Year of publication
1994
Pages
121 - 125
Database
ISI
SICI code
0032-0781(1994)35:1<121:COCCAD>2.0.ZU;2-U
Abstract
Three soya-bean (Glycine max) cell-wall enzymes (beta-glucosidase, pec tin methyl esterase and phosphatase) have been found to be glycoprotei ns. The polyclonal antibodies raised against pectin methyl esterase an d beta-glucosidase lacked specificity, cross-reacted highly with nativ e enzymes and also both reacted with pure soya-bean phosphatase, horse radish peroxidase and honeybee venom phospholipase A2. They did not re act with either non-glycosylated bacterial phosphatase or deglycosylat ed cell-wall enzymes. The two antisera contained both non-specific ant i-glycan antibodies and specific anti-polypeptide antibodies that were quantified. Antiglycan antibodies specific to alpha1-3 fucose and bet a-2 xylose were detected in both antisera and were separated and quant ified. The occurrence of terminal fucose (and mannose) was confirmed w ith specific lectins. These results indicate that most of the common g lycan epitopes probably correspond to the asparagine-linked complex gl ycan previously detected in several glycoproteins of plants as well as in those of molluscs and insects.