Detecting the enzymatic synthesis of a-galactosyl trisacchride by using a quartz crystal microbalance

AEI 24

Mingchuan Huang, mhuang@chemistry.ohio-state.edu and Peng George Wang, pgwang@chemistry.ohio-state.edu. Department of chemistry, the Ohio State University, 100 W. 18th Avenue, Columbus, OH 43210
Enzymatic reaction between UDP galactose and immobilized lactose was studied by using a quartz crystal microbalance. Lactose was tailored with a thiol linker that formed self-assembled monolayers (SAMs) on the gold surface of QCM. Negative frequency shift was observed with the addition of UDP galactose and alpha 1,3-galactosyltransferase to the lactose surface. The formation of alpha-Galactosyl trisacchride was confirmed by measured binding of the polyclonal anti-Gal antibody with formed alpha Gal epitope.
 

Academic Employment Initiative
8:00 PM-10:00 PM, Monday, 11 September 2006 Moscone Center -- Hall D, Sci-Mix

Academic Employment Initiative

The 232nd ACS National Meeting, San Francisco, CA, September 10-14, 2006