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Extra info for Methods of Biochemical Analysis, Volume 33
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Basic proteins are eluted most efficiently in high-pH buffers (Szewczyk and Kozloff, 1985). In summary, there are many factors that affect the final gel replica. When possible, it is preferable to use a gradient electric field (50-10 V, 200 mA) and a low ionic strength buffer with no methanol. Under such conditions reasonably efficient transfers can be achieved in a matter of 2-3 h. VIII. STAINING OF BLOTS The visualization of the transferred protein pattern immobilized on the matrix can be useful in evaluating the quality of transfer and, more important, to allow the correlation of the eventual signal to a specific band.
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.
Surprisingly, not many people test to see the separation obtained under much milder conditions-for example, by not heating the sample, by omitting reducing agents, or by decreasing the detergent concentration. 5% SDS or less. Running the gel in the cold is also advantageous. For this purpose, Delepelaire and Chua (1979) developed lithium dodecylsulfate/polyacrylamide gels. , 1982, 1983). Unexpected factors can also have detrimental effects. Bromphenol blue can sometimes act as a cross-linker and alkylate some proteins.