HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) 091165.Supplemental Data Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in Web of Science Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Garbett, N. C. Articles by Chaires, J. B. Search for Related Content PubMed Articles by Garbett, N. C. Articles by Chaires, J. B. Related Collections Oak Ridge Conference Proteomics and Protein Markers

Interrogation of the Plasma Proteome with Differential Scanning Calorimetry

(¹ James Graham Brown Cancer Center and ² Department of Pathology and Laboratory Medicine, University of Louisville, Louisville, KY;

^aaddress correspondence to this author at: Department of Pathology and Laboratory Medicine, University of Louisville, Louisville, KY 40292; fax 502-852-1771, e-mail jmiller@louisville.edu)

The first 300 words of the full text of this article appear below.

Human plasma is a complex fluid that contains more than 3000 individual proteins and peptides in quantities ranging from nanograms to tens of grams per liter (1)(2). The plasma proteome and peptidome(3) hold great promise for disease diagnosis and therapeutic monitoring(4)(5). In recent years proteomics has focused primarily on analysis of low-abundance proteins by use of high-resolution methods such as 2-dimensional electrophoresis(6) and mass spectrometry(7). These methods have identified changes in the composition of low-abundance proteins and peptides in plasma that correlate with particular diseases. Typically no single protein emerges from such analyses as a wholly reliable biomarker. Instead changes in the pattern of proteins and peptides often serve as the best diagnostic indicator for a particular disease. In addition, many components of the peptidome were found to be complexed with more abundant serum proteins, especially human serum albumin and immunoglobulins. These findings led to the concept of the "interactome"(8).

Currently, the routine clinical laboratory procedures that are used to assess major components of the proteome include protein electrophoresis (PE) and immunofixation electrophoresis. Modern differential scanning calorimetry (DSC) provides a direct means for detecting what is perhaps the most fundamental property of biochemical reactions, heat changes, and can reliably measure heat changes of 0.1 µcal. In a typical DSC experiment, an aqueous solution of protein is heated at a constant rate in the sample cell alongside an identical reference cell that contains only the solvent (buffer). Thermal balance between the sample and reference cells is maintained by electrically powered feedback heaters. Any chemical process in the sample cell that absorbs or releases heat results in a thermal imbalance. The power applied by the feedback heaters provides a direct measure of heat capacity changes accompanying . . . [Full Text of this Article]