Ultracytochemistry of glycoconjugates in pig duodenal gland.

To elucidate the ultrastructure, glycoprotein profile and site of glycosylation of glandular cells in relation to the functional polarity of the organelles, swine duodenal tissue was embedded in glycol methacrylate and subsequently stained for periodic acid thiocarbohydrazide silver proteinate (PA-TCH-SP), high iron diamine (HID)-TCH-SP, low iron diamine (LID)-TCH-SP, ninhydrin T-TCH-SP and five peroxidase-labeled lectins. The secretory granules in the duodenal gland cells were electron lucent with a 200 nm to 500 nm electrondense core. Glycoconjugates were confined to the secretory granules and elements of the Golgi complex. Protein activity was located only in the electron dense core. Achivementestic staining pattern for Concanavalin A (Con A), peanut agglutinin (PNA), Ulex europaeus agglutinin-I (UEA-I), wheat germ agglutinin (WGA) and soybean agglutinin (SBA) was observed in stained secretory granules and the Golgi apparatus. A few cis cisternae were stained with SBA and UEA-I. Trans cisternae were stained with WGA and PNA. Con A reacted with seromucous granules and rough endoplasmic reticulum. These observational findings suggest that these are seromucous cells. The Golgi apparatus is the site of glycosylation and can be divided into two distinct compartments.