Abstract
A method for the covalent binding of rat liver UDP-glucuronosyltransferase to a cyanogen bromide-activated agarose matrix is described. the rat liver microsomal fraction was solubilized with 8 mM 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate (CHAPS); 90% of the microsomal protein was solubilized. Some 50–60% of this protein became bound covalently to the activated agarose matrix. the immobilized UPD-glucuronosyltransferase remained completely active for 50 days when stored at 4° in a 20% (v/v) glycerol buffer (pH7.4). the immobilized enzyme has a temperature optimum around 37°, and a broad pH optimum (pH 5–7.4). the enzyme displayed linear kinetics over a period of 1 hr; it conjugates a large variety of substrates.
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