ABSTRACT
The purification of enzymes can exploit either their general protein characteristics (e.g., when using a physical separation or a method based on relatively nonspecific interactions) or their specific biological interactions (e.g., as employed in bioselective separations). In practice, these two recognition modes are often used sequentially. This is the case because attempts at bioselective separations at an early stage in the purification process may encounter nonspecific binding, while physical separations or those based on nonspecific interactions are usually inadequate to distinguish between proteins that have similar physical properties.
