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Titlebook: New Protein Techniques; John M. Walker Book 1988 Springer Science+Business Media New York 1988

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Direct Immunoprecipitation of Protein, used effectively to purify the antigen protein. The method described here is of the latter sort and has advantages of simplicity and rapidity both over ELISA and blotting techniques, on the one hand, and indirect precipitation techniques on the other.
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Isoelectric Focusing Under Denaturing Conditions,tively strong charge of the dodecyl sulfate ion, which resulted in very good correlation (for most, but not all, proteins) between electrophoretic mobility and molecular weight (.. in Vol. 1 of this series).
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The Bradford Method for Protein Quantitation, this series) has been widely used, but is susceptible to interference from a wide range of compounds commonly present in biological extracts. Although interference can be avoided by trichloracetic acid precipitation of the protein prior to assay, this lengthens the procedure.
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Enzymatic Methods for Cleaving Proteins,s of peptide mapping, primary structure determination, and preparation of particular fragments for studies relating structure and function. Proteinases (or more specifically endo-proteinases) are commonly used to generate peptides for these purposes, but the number of particularly useful and commerc
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Chemical Cleavage of Proteins,t 110°C for 24 h hydrolyzes a polypeptide to a mixture of single amino acids. Others show some discrimination, however, as to the precise nature of the amino acid residues around the bond to be broken. Some of these methods are sufficiently specific to be of use, for instance, for generating peptide
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