ISSN:
0173-0835
Keywords:
Human saliva
;
Glycoproteins
;
Lectins
;
Sodium dodecyl sulphate-polyacrylamide gel electrophoresis
;
Chemistry
;
Biochemistry and Biotechnology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Biology
,
Chemistry and Pharmacology
Notes:
Human parotid salivary glycoproteins separated by gradient sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) and electroblotted onto nitrocellulose have been investigated using a battery of biotinylated lectin probes of characterized sugar specificity. Lectin binding, detected on blots using avidin-biotin complex (ABC) and a chemiluminescence generating substrate, was recorded on photographic film and compared with the original fluorescein isothiocyanate (FITC) stained blots or with Coomassie Brilliant Blue R-250-stained gels run in parallel. A number of glycoprotein bands which were undetected by protein stains or the periodic acid Schiff reaction were revealed by lectins. Binding by lectins from Concanavalia ensiformis, Lens culinaris, Limax flavus, Phaseolus vulgaris, Ricinus communis, Triticum vulgaris, Lotus tetragonobulus and Ulex europaeus indicated that sialylated and fucosylated triantennary and bisected, N-linked complex sugar chains were present on many glycoproteins in addition to the major glycosylated proline-rich glycoprotein (GI). Binding with lectins from Arachis hypogaea and Dolichos biflorus indicated that the O-linked sugar chains were confined to the α-heavy chain of Ig A. Comparison of lectin binding in samples from five healthy individuals revealed differences in a number of flycoproteins in addition to the previously characterized GI and CON 1/CON 2 polymorphisms and demonstrated that the H blood group antigen was expressed mainly on GI in parotid saliva. This study will be used as a basis upon which to study salivary glycoproteins in diseases affecting parotid glands.
Additional Material:
6 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/elps.1150170116
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