This method involves the irreversible formation of a complex between ?labeled cu-bungarotoxin and the acetylcholine receptor in either its membranebound or purified state. The separation of the labeled toxin-receptor complex from unreacted toxin is accomplished by chromatography on carboxymethylcell
Quantitative assay of the binding of small molecules to protein: Comparison of dialysis and membrane filter assays
โ Scribed by Julia E. Lever
- Publisher
- Elsevier Science
- Year
- 1972
- Tongue
- English
- Weight
- 656 KB
- Volume
- 50
- Category
- Article
- ISSN
- 0003-2697
No coin nor oath required. For personal study only.
๐ SIMILAR VOLUMES
Although the Bradford protein estimation assay has found wide distribution, it has a number of drawbacks, which in some cases have been shown to produce erroneous results upon comparison to other, more precise, methods for protein estimation. It was found that the underestimation of the protein cont
New filter assay methods are presented for quantitating both cytoplasmic and nuclear forms of the estrogen receptor protein. These methods exploit the strong adsorption of this protein to glass-fiber filters, which appears to occur without loss of steroid binding affinity. A "direct assay protocol"
A flow cytometric method to quantify the Granulocyte-macrophage colony-stimulating factor receptor (GM-CSFr) on human cells is described. The number of GM-CSFr binding sites on human neutmphils was assessed by using Merent bead standards. Results were compared with those from conventional receptor q
The Coomassie brilliant blue Cl assay for proteins described by Bradford (1976) (Ana!. Biochem. 72, 248) was reexamined. It was found that the extinction coefficient of the dye-protein complex solution remained constant over the protein concentration range of 0.8 to 10 &ml of solution. This unchangi