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By David Glick

An encyclopaedia of tools in biochemical research, this contemporary sequence retains biochemists and analytical chemists abreast of experimental thoughts and enhancements in biochemical strategies and instrumentation.

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Bromphenol blue can sometimes act as a cross-linker and alkylate some proteins. Therefore one should attempt to obtain reasonable resolution with minimal modification of the proteins. B. , Wetlaufer and Ristow, 1973; Anfinsen and Scheraga, 1975; Wetlaufer, 1981; Kim and Baldwin, 1982). However, no simple formula exists, especially for membrane-associated proteins. A number of protocols have been suggested, yet none have been rigorously examined and controlled. After SDS-PAGE, one usually wants to remove excess SDS and allow the protein to refold in situ.

Colloidal iron has been used for the nylon-based membranes. Immunodetection of hapten-derivatized proteins can also provide a general protein stain. IX. QUENCHING After protein transfer, the blots are probed. However, because the probe itself can bind nonspecifically to the immobilizing matrix, an PROTEIN BLOTTING: A MANUAL 25 intermediate step must be introduced, namely quenching. This is the process of blocking all unoccupied binding sites of the filter. , BSA, hemoglobin, gelatin, fetal calf serum, milk).

38. Walker et al. Wilkins et al. P. Wolff et al. (1985). The spectrum of “ligands” that have been used is extremely broad. , 1984) and as large as spectrin (Davis and Bennett, 1983) have been employed. It is remarkable that blots can be probed with intact organisms. Hayman et al. (1982, 1983, 1985) showed that adherence proteins can be identified via blotting. , 1985). , 1986). The successful application of ligand overlay indicates that many molecular associations may rely on relatively short linear amino acid sequences or that sufficient structure can be preserved or regained during the electrophoretic chromatography and blotting.

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