1. 0-Substituted Serine and Threonine Residues in Acetylcholine Receptor Protein from Torpedo californica. 2. Synthesis of a New Fluorescent Probe for Ligand Binding to Acetylcholine Receptor from Torpedo californica

Author: Eisenach, James Conrad

Year: 1978

Degree: Master's thesis

Advisor: Raftery, Michael A.

Committee Member: Unknown, Unknown

Option: Chemistry

DOI: 10.7907/0rts-8j78

Abstract

Part I deals with chemical studies performed on purified acetylcholine receptor from Torpedo Californica
designed to document the presence and nature of 0-substituted serine and threonine residues. Treatment of receptor with methylamine in base and analysis of the products formed showed 24 0-substituted serine residues per 300,000 daltons protein and the presence of 0-substituted serine in all four subunits. The amount of 0-substituted threonine present in receptor was estimated by treatment with alkaline sodium borohydride, suggesting 25 such residues per 300,000 daltons protein. Evidence is presented suggesting that at least half of this 0-substitution to serine and threonine is accounted for by 0-glycosyl linkage to carbohydrate chains of short length.

Part II deals with synthesis of a fluorescent probe for ligand binding to acetylcholine receptor. The probe synthesized contains a highly fluorescent moiety and a photo-induced reactive azide group, and is a suicide probe in that it contains an acetylcholine moiety which should direct it to the ligand binding site. This latter moiety can be removed after reacting the azide to leave a fluorescent probe located adjacent to the ligand binding site.

Files