Abstract
In this chapter we consider the properties of proteins isolated for their native function. The focus is on the native state of the protein and the subtle way in which evolution has tailored polypeptide chains to produce highly specific secondary, tertiary, and quarternary structure. For some proteins, this characterization is complete to atomic resolution (e.g., lysozyme, hemoglobin). This is because of the major efforts and technical advances in molecular biology in recent decades. It is important to recognize that for biochemical use, however, isolated material can be equally well characterized in terms of its “activity,” i.e., the ability to perform its intended function. The latter approach does not necessarily refer to any molecular configuration or even to the presence of molecules at all. This is particularly true for pharmacology, in which functional characteristics are largely pragmatic. For example, the active macromolecule in antisera is identifiably proteinaceous, but the British Pharmacopeia characterizes scorpion venom antiserum as a serum obtained from healthy animals having not more than 17.0 wt/vol % protein, and sufficient potency to neutralize the maximum amount of venom from a single sting (1).
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Lillford, P.J. (1988). Characterization and Functional Attributes of Protein Isolates. In: Franks, F. (eds) Characterization of Proteins. Biological Methods. Humana Press. https://doi.org/10.1007/978-1-59259-437-5_18
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DOI: https://doi.org/10.1007/978-1-59259-437-5_18
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