Labeling of Sweet Taste Binding Sites using a Colloidal Gold-Labeled Sweet Protein, Thaumatin

Authors

Albert I. Farbman, Northwestern University
Carolyn K. Ogden-Ogle, Northwestern University
Göran Hellekant, University of Wisconsin
Scott R. Simmons, University of Wisconsin
Ralph M. Albrecht, University of Wisconsin
H. van der Wel, University of Wisconsin

Abstract

Thaumatin, an intensely sweet tasting protein, was bound to colloidal gold and applied to the taste bud-bearing foliate papillae of Rhesus monkeys. Examination of thin sections of taste pores showed that gold particles were bound to merocrine secretions of Type I taste bud cells, to some cell remnants of lysed cells, and, most importantly, to small, membrane bounded blebs of cytoplasm. These blebs are thought to be shed into the pore from the tips of taste bud cell microvilli, particularly those arising from Type II cells. The binding of gold particles to microvillus tips and to the blebs suggest that this may be an important means by which taste bud cells rid themselves of taste stimulus-receptor complexes.

Recommended Citation

Farbman, Albert I.; Ogden-Ogle, Carolyn K.; Hellekant, Göran; Simmons, Scott R.; Albrecht, Ralph M.; and van der Wel, H. (1986) "Labeling of Sweet Taste Binding Sites using a Colloidal Gold-Labeled Sweet Protein, Thaumatin," Scanning Microscopy: Vol. 1: No. 1, Article 32.
Available at: https://digitalcommons.usu.edu/microscopy/vol1/iss1/32