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Biochemical pharmacology

Immobilization of solubilized UDP-glucuronosyltransferase from rat liver microsomes to Sepharose 4B.


PMID 1632822

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 degrees in a 20% (v/v) glycerol buffer (pH 7.4). The immobilized enzyme has a temperature optimum around 37 degrees, 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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C9210
Cyanogen bromide-activated Agarose, lyophilized powder