Showing papers on "Bradford protein assay published in 1979"
TL;DR: The method is applicable to protein assay in the presence of other nonionic detergents under certain conditions and allows the assay of both water-soluble and hydrophobic protein in solutions containing concentrations of Triton X-100 up to at least 4% (v/v).
39 citations
TL;DR: The suitability and reliability of this method for the determination of the native zinc content of serum alpha-2-M is supported by the experimental findings that this procedure does not cause exogenous zinc contamination and is not disruptive to protein-metal interaction.
17 citations
TL;DR: The variation in the sensitivity of proteins to some commonly used protein assay procedures was estimated by a calculation of the ideal titer per unit weight of protein for a sample of 350 proteins.
5 citations
TL;DR: This chapter describes the biotin-binding protein present in egg yolk, which is based on the temperature-accelerated exchange of bound biotin for free [ 14 C]biotin, and the purification procedure for biotin -binding protein of egg yolks is described in the chapter.
Abstract: Publisher Summary This chapter describes the biotin-binding protein present in egg yolk. The assay is based on the temperature-accelerated exchange of bound biotin for free [ 14 C]biotin. The procedure is, therefore, useful for biotin-binding proteins with no free binding sites. The purification procedure for biotin-binding protein of egg yolk is described in the chapter. All buffers used are potassium phosphate, pH 7.2, at the concentration given. The procedure is for 5 dozen eggs. The eggs are cracked and the white and yolks are separated. The yolks are broken and 1.5 times the yolk volume in distilled water is added. The diluted yolk is well stirred. This solution is centrifuged at 13,200 g for 30 minutes. The supernatant is collected, and solid NaCl is added to make the solution 1 M in salt. After the salt has completely dissolved, the solution is poured into centrifuge bottles, two-third the solution volume in 1-butanol is added, and the mixture is shaken vigorously. The centrifugation of the resulting emulsion at 13,200 g for 15 minutes causes a lipid-free aqueous phase and a lipid-rich organic phase to form, with a solid layer of precipitated protein at the interface. The chapter discusses the properties of the biotin-binding protein.
4 citations