Distribution of lectin-binding sites in oxyntic and chief cells of isolated XXXX gastric glands.

@entity9377 @entity95 @entity48777 @entity3953 @entity3913 @entity3649 @entity1460 @entity3505
The distribution of lectin-binding sites in oxyntic and chief cells of isolated @entity95 gastric glands was determined with seven fluoresceinated lectins, to ascertain which lectins might best be used in the biochemical characterization of cell membranes and glycoproteins of these two cell types. Oxyntic cell canaliculi were labeled by @entity3505 germ, Helix pomatia, and peanut lectins, suggesting a predominance of @entity48777 . Tubulovesicles were heavily stained by @entity3505 germ, Helix pomatia, and @entity9377 I lectins, indicative of @entity48777 - and @entity3649 -containing glycoconjugates. Diffuse oxyntic cell cytoplasmic staining was observed with the @entity3913 -binding lectin concanavalin A. This lectin, along with @entity3505 germ, @entity1460 , Helix pomatia, and @entity9377 I lectins, bound to oxyntic cell basolateral membranes, indicating @entity3913 , @entity48777 , and @entity3649 residues. Chief cell apical membranes were labeled with peanut, @entity9377 I, Helix pomatia, and Ulex europaeus lectins, suggesting a predominance of @entity48777 , @entity3649 , and @entity3953 residues. None of the lectins demonstrated any significant affinity for chief cell cytoplasm or basolateral membrane. Ulex europaeus agglutinin-binding sites were additionally concentrated in lateral intercellular spaces. The results of this study indicate that the range of utility of isolated @entity95 gastric glands can be expanded to include histochemical work. In addition, the data suggest the applicability of lectin affinity chromatography in the isolation and characterization of oxyntic and chief cell membranes and glycoproteins.
