## Mechanical stabilization of large pore acrylamide gels by addition of linear polyacrylamide Linear polyacrylamide has been used to increase the tensile strength and stability of low percentage acrylamide gels in the range of 2.5 to 6.0 % w/v acrylamide. This added strength allows handling and st
A solid-phase method for the quantitation of protein in the presence of sodium dodecyl sulfate and other interfering substances
β Scribed by J.B. Sheffield; David Graff; H.P. Li
- Publisher
- Elsevier Science
- Year
- 1987
- Tongue
- English
- Weight
- 558 KB
- Volume
- 166
- Category
- Article
- ISSN
- 0003-2697
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β¦ Synopsis
We describe a simple assay for small amounts of protein that is insensitive to sodium dodecyl sulfate (SDS) or many common interfering substances including Tris and reducing sugars. For this reason. it is particularly useful in the analysis of protein content of samples prior to SDS electrophoresis. The assay consists of the following steps: (i) absorption of protein to nitrocellulose; (ii) fixation of the bound protein with methanol: (iii) staining of the bound protein with amido black: and (iv) elution and spectrophotometric measurement of the bound dye. The assay is sensitive to as little as 0.5 pg of protein in 1 @I of solution. Although SDS does not interfere appreciably with measurement, Nonidet-P40 does. o 1987 Academic PT~SS. IIIC.
π SIMILAR VOLUMES
A method for protein determination in one- and two-dimensional electrophoresis sample buffer is presented. Accurate quantitation of protein in two-dimensional electrophoresis sample buffer (9.5 M urea, 2% Nonidet P-40, 2% carrier ampholytes, and 5% 2-mercaptoethanol) required removal of carrier amph