In this study colloidal gold methodologies that allow the lectin affinity patterns in the mouse parotid gland to be studied by postembedding techniques were addressed. DBA, Con A, PNA, WGA and LTA lectins conjugated with gold particles or horseradish peroxidase for a direct or indirect technique of binding were used. Thin sections were obtained from tissue embedded in the acrylic hydrophilic resins Bioacryl and Lowicryl K4M. The most satisfactory results originated from sections infiltrated in Bioacryl and submitted to the indirect technique of binding. The mouse parotid gland appeared to be composed of polymorphous secretory granules differentially stained by lectins. The glycosylated components of acinar cells reacted intensely, and gold particles specified the ultrastructural distribution of lectin affinity sites reflecting the location of beta-galactose, alpha-N-acetylgalactosamine, beta-N-acetylglucosamine, alpha-D-mannose, and alpha-L-fucose in the electron-dense or electron-lucent areas of bizonal, mottled, and target granules.
Glycocytochemistry of the mouse parotid gland. Investigation by lectin-gold techniques on Bioacryl and Lowicryl K4M embedded specimens
MENGHI, Giovanna;MARCHETTI, Luigi;GABRIELLI, Maria Gabriella;MATERAZZI, Giovanni
1996-01-01
Abstract
In this study colloidal gold methodologies that allow the lectin affinity patterns in the mouse parotid gland to be studied by postembedding techniques were addressed. DBA, Con A, PNA, WGA and LTA lectins conjugated with gold particles or horseradish peroxidase for a direct or indirect technique of binding were used. Thin sections were obtained from tissue embedded in the acrylic hydrophilic resins Bioacryl and Lowicryl K4M. The most satisfactory results originated from sections infiltrated in Bioacryl and submitted to the indirect technique of binding. The mouse parotid gland appeared to be composed of polymorphous secretory granules differentially stained by lectins. The glycosylated components of acinar cells reacted intensely, and gold particles specified the ultrastructural distribution of lectin affinity sites reflecting the location of beta-galactose, alpha-N-acetylgalactosamine, beta-N-acetylglucosamine, alpha-D-mannose, and alpha-L-fucose in the electron-dense or electron-lucent areas of bizonal, mottled, and target granules.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.