Abstract
The present study examined the liquid membrane transport of the cationic protein cytochrome c, using the macrocyclic compound calix[6]arene, which is a carboxylic acid derivative, as a carrier. The transport rate was governed by carrier concentration and the pH gradient between the feed and the receiving phases, as well as the salt concentration in the aqueous phases. Transport of cytochrome c was examined using a series of calix[ n]arene carboxylic acid derivatives ( n = 4, 6 and 8). Cytochrome c successfully permeated membranes in the presence of the calix[6]arene derivative. Liquid membrane separation of cytochrome c from a mixture of cationic proteins was demonstrated under optimal conditions. Cytochrome c was selectively extracted by the calix[6]arene carboxylic acid derivative and 77% of the extracted cytochrome c was recovered into the receiving phase. In this liquid membrane system, which discriminates between the number of lysine residues on the surface of proteins, cationic proteins with similar molecular weights and p Is were separated with macrocyclic compounds.
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