By John M. Walker
Univ. of Hertfordshire, Hatfield, united kingdom. offers a cross-section of analytical innovations standard for proteins and peptides. every one bankruptcy opens with an outline of the fundamental thought at the back of the strategy being defined. define structure. prior variation: c1996. Hardcover, softcover additionally to be had.
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Extra resources for The Protein Protocols Handbook
Sample text
Acid and L-asparagine failed to yield products that absorbed at 358 nm (Fig. 1B and data not shown). Nucleotides (ATP, CTP, GTP, TTP, UTP), RNA, and DNA also failed to yield products that absorbed at 358 nm. These investigations led us to propose that the 358 nm absorption peak observed after nitric acid solubilization of cells likely primarily reflects the tyrosine content of cellular proteins. To understand better the chemistry responsible for these observations, we solublized L-tyrosine in nitric acid for 1 h.
116, 53–64. 7. Stoscheck, C. M. (1990) Increased uniformity in the response of the Coomassie Blue protein assay to different proteins. Analyt. Biochem. 184, 111–116. 8. Spector, T. (1978) Refinement of the Coomassie Blue method of protein quantitation. 5 to 50 µg of protein. Analyt. Biochem. 86, 142–146. 9. Pande, S. V. and Murthy, M. S. R. (1994) A modified micro-Bradford procedure for elimination of interference from sodium dodecyl sulfate, other detergents, and lipids. Analyt. Biochem. 220, 424–426.
Microassay 1. 0 µg of protein/mL, add 1 mL of SWR. 2. Incubate at 60°C for 1 h. 3. Cool, and read the absorbance at 562 nm. 4. Notes 1. Reagents A and B are stable indefinitely at room temperature. They may be purchased ready prepared from Pierce, Rockford, IL. 2. The sensitivity of the assay can be increased by incubating the samples longer. Alternatively, if the color is becoming too dark, heating can be stopped earlier. Take care to treat standard samples similarly. 3. Following the heating step, the color developed is stable for at least 1 h.