A microfluidic-based method for recovering enhanced enzymatic activity of membrane bound proteins from isolated rat liver cells

ANYL 152

Mark David Goldberg, Department of Chemistry and Biochemistry, California State University Los Angeles, 5155 State University Drive, Los Angeles, CA 90032, Frank A Gomez, cufomadu@yahoo.com, Department of Chemistry and Biochemistry, California State University, 5151 State University Drive, Los Angeles, CA 90032-8202, Naresh Menon, Director of Biotechnology, Physical Optics Corporation, 20600 Gramercy Place, Bldg 100, Torrance, CA 90501-1821, and Greg Zeltser, Biotechnology, Physical Optics Corporation, 20600 Gramercy Place, Bldg 100, Torrance, CA 90501-1821.
It is well known that protein structure and function are linked, and that a protein's function, particularly a membrane bound protein, requires the hydrophobic environment of the membrane to perform a specific function. To date, our current understanding of many proteins is hindered by difficulties in separating and isolating membrane bound proteins without changing their structure, directly impacting their enzymatic function. Our studies utilized microfluidic chips fabricated from polydimethylsiloxane (PDMS) to isolate rat liver proteins from their membranes. Our results revealed a 2X increase in measured enzymatic activity when compared to the enzymatic activity of proteins isolated by conventional membrane extraction procedures. This data suggests that proteins isolated from membranes using PDMS chips retain their three dimensional structure, which enhances their in vitro membrane-free enzymatic activity, making otherwise insoluble proteins soluble.
 

General Papers
7:00 PM-9:00 PM, Sunday, 10 September 2006 Moscone Center -- Hall D, Poster

Division of Analytical Chemistry

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