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Chiral-Merck

Description

Hermansson described the use of natural proteins immobilized onto a silica support for chiral separations in 1983 (1). Proteins contain a large number of chiral centers of one configuration, and many other sites that contribute to the general retention process. CHIRALPAK AGP has the broadest range of selectivity of all protein phases currently available. CHIRALPAK AGP phase uses ?1-acid glycoprotein (AGP) as the chiral selector immobilized on spherical 5 ?m silica particles. Bonded AGP is a very stable protein that tolerates pure organic solvents, elevated temperatures and pH values from 4 to 7. Operated in reversed-phase mode, CHIRALPAK AGP column separates enantiomers of an extremely broad range of drug substances, such as acids, amines and neutral compounds. The enantioselectivity and retention can easily be regulated by mobile phase pH and ionic strength, and the nature and concentration of the organic modifier.

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