Measurement of microgram quantities of protein by a generally applicable turbidimetric procedure
β Scribed by Juan C. Vera
- Book ID
- 102986333
- Publisher
- Elsevier Science
- Year
- 1988
- Tongue
- English
- Weight
- 844 KB
- Volume
- 174
- Category
- Article
- ISSN
- 0003-2697
No coin nor oath required. For personal study only.
β¦ Synopsis
A modified turbidimetric method for protein determination which involves the use of trichloroacetic acid as the precipitating agent is described. Maximal turbidity develops in less than 30 min and is stable for at least 120 min. A linear relationship between turbidity at 340 nm and protein concentration is observed between 2 and 40 micrograms protein. Sodium dodecyl sulfate is added to avoid the interference by nonionic and cationic detergents and lipids and to decrease the protein-to-protein variation. The use of cetyltrimethyl ammonium bromide provides a two-step procedure to correct for the contribution of contaminating nucleic acid. Many compounds which interfere with other protein quantitation methods have no effect on this system. The interference of commonly used reagents as sucrose and urea can be easily corrected. This procedure compared favorably with the most widely used protein quantitation methods in simplicity, sensitivity, and specificity.
π SIMILAR VOLUMES
A technique has been perfected for measuring the sedimentation coefficient of microgram quantities of a reduced protein in 6 M guanidine hydrochloride. The protein is sedimented through a gradient of 5-8 M guanidine-HCl in the presence of dithiothreitol in a SW 50.1 swinging-bucket rotor. Run condit
The flexibility of surface loops plays an important role in protein-protein and protein-peptide recognition; it is commonly studied by Molecular Dynamics or Monte Carlo stimulations. We propose to measure the relative backbone flexibility of loops by the difference in their backbone conformational e