Purification and Characterization of Esterase 1F, the Albumin Esterase of the House Mouse (Mus musculus)

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Abstract
Esterase 1F was isolated from mouse serum and purified by ion-exchange chromatography, isoelectrofocusing and molecular sieve chromatography. It is considered to be a glycoprotein with an apparent MW of 75,000. The equivalent weight (.apprxeq. 77,000 .times. g/mol) was estimated by titration of the catalytic site with diethyl p-nitrophenyl phosphate. The Km and the catalytic constant kcat of the enzyme for 4-nitrophenyl hexanoate were determined. Esterase 1F is characterized by its ability to split a wide spectrum of substrates and its relatively low turnover rates towards the substrates tested. It belongs to the isozyme system of carboxylesterase (EC 3.1.1.1) coded for by chromosome 8. Esterase 1F was compared with 3 other genetically related isozymes, esterase 2, esterase 7 and esterase 9, with respect to some physical and catalytic properties.

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