Isolation and characterization of a butyrylesterase from human erythrocytes - Axenfors, B.; Andersson, I.; Augustinsson, K.-B. (Elsevier)
Human erythrocytes contain a butyrylesterase which, judging from the ease with which it can be solubilized, is present in the cytoplasm of these cells. This enzyme has been isolated and a number of its properties characterized. The purified enzyme hydrolyzed butyryl esters with both a lower K"m and higher V than is seen with esters containing longer or shorter acyl groups. It has a molecular weight of 320 000 and an isoelectric point of 4.1. This low isoelectric point is apparently a result of the relatively high content of glutamic and aspartic acids. The stability of the isolated butyrylesterase has been examined under a number of different conditions. The enzyme is inhibited by low conconcentrations of Hg^2^+, Cd^2^+, Zn^2^+ and the organophosphorus compound Mipafox, but is insensitive to eserine. The properties of this butyrylesterase, including its ability to hydrolyze thiocholine esters at a relatively rapid rate (albeit with a high K"m), are a mixture of those expected for an arylesterase and a cholinesterase.
http://linkinghub.elsevier.com/retrieve/pii/0005-2744(79)90202-X
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