Comparative study of colorimetric methods for analysis of water-soluble and immobilized proteins and peptides

BIOL 202

Nataliya M. Samoshina, nsamoshina@pacific.edu and Vyacheslav V. Samoshin, vsamoshin@pacific.edu. Department of Chemistry, University of the Pacific, 3601 Pacific Ave., Stockton, CA 95211
A comparison of the use of several chromogenic assays with the same sample population has showed that only the Hartree assay is generally applicable to quantitative determination of various peptides and proteins. The quantities of water-soluble and immobilized proteins and peptides have been measured using Bradford, Smith (BCA) and Hartree assays in the presence of various substances that are commonly used for isolation, purification, stabilization, and immobilization of proteins. Some of the studied compounds (SDS, EDTA, Na3PO4, Triton X-100, sucrose, Brij-58, glycerol, urea, glutaraldehyde, NaN3) caused either positive or negative deviations of the results. For immobilized proteins, a good correlation was found between the results of the Hartree and Smith assays, while the Bradford assay was shown to be inapplicable.
 

Enzymes
4:30 PM-6:30 PM, Wednesday, 13 September 2006 Moscone Center -- Hall D, Poster

Division of Biological Chemistry

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