( T Slyker B Gillece-Cas...)Sample Preparation Solutions for Cellular Protein Fractionation Poster, Rev A
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T Slyker, B Gillece-Castro, M Nguyen, L Sapp, MG Brubacher, and WB Strong
Presented by the Authors at The Association of Biomolecular Resource
Facilities (ABRF)
February 1013, 2003
Denver, Colorado
Abstract
2-D gel electrophoresis (2DE) is a widely used, proven method for proteome
analysis. The quality and value of the information obtained from a 2DE
experiment is highly dependent upon the initial sample preparation. In
order to identify the most complete array of cellular proteins it is often
necessary to reduce the complexity of the protein sample. A strategy for
reduction in sample complexity is especially important when analysis of
low-abundance and membrane proteins is the goal. Ideally the method(s)
employed should be simple, reproducible, general to a wide variety of
cell types, and result in a low conductivity protein sample that is free
of substances that interfere with 2DE. With these aims in mind, we will
present several solutions for convenient and efficient extraction of cellular
proteins into discrete, more easily manageable fractions that are enriched
in certain classes of proteins such as cytosolic, nuclear, membrane, and
signaling. The majority of these procedures are intended to provide tools
that simplify the preparation of membrane proteins that are generally
considered difficult to isolate. These proteins are of considerable interest
due to their roles in signal transduction and cell-to-cell interactions
among other functions. 2DE and MALDI peptide mass fingerprinting data
will be presented to illustrate the effective application of these techniques
to improved sample prefractionation and protein identification.
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