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
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.