Abstract
Utilization of high-performance liquid chromatography (HPLC) in peptide/protein chemistry has become widespread. The technique is being used for amino acid analysis (1,2,3), for peptide isolation from natural sources (4,5) or from enzymatic/chemical cleavages (6,7), for the identification of products arising from Edman degradations (8,9) and for determining the specificity of chemical cleavage methods (10). Its application in the chromatography of larger peptide fragments or proteins has been limited, in part, by the lack of suitable column packings. Until only recently most commercially available reverse phase packings exhibited nonspecific adsorption and/or reduced resolution. However, some proteins have been chromatographed under a variety of conditions on quite different column supports.
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Wilson, K.J., Berchtold, M.W., Zumstein, P., Klauser, S., Hughes, G.J. (1982). Reverse Phase High-Performance Liquid Chromatography for Protein Purification: Insulin-Like Growth Factors, Ca2+- Binding Proteins and Metallothioneins. In: Elzinga, M. (eds) Methods in Protein Sequence Analysis. Experimental Biology and Medicine, vol 3. Humana Press. https://doi.org/10.1007/978-1-4612-5832-2_33
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DOI: https://doi.org/10.1007/978-1-4612-5832-2_33
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