Open AccessPurification and Characterization of Esterase 1F, the Albumin Esterase of the House Mouse ( Mus musculus )
Author(s) -
OTTO Johannes,
RONAI Adam,
DEIMLING Otto
Publication year - 1981
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1981.tb05331.x
Subject(s) - esterase , carboxylesterase , isozyme , michaelis–menten kinetics , chemistry , turnover number , biochemistry , enzyme kinetics , enzyme , chromatography , titration , enzyme assay , active site , organic chemistry
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 molecular weight of 75000. The equivalent weight (∼ 77000 × g /mol) was estimated by titration of the catalytic site with diethyl p ‐nitrophenyl phosphate. The Michaelis constant K m and the catalytic constant k cat , 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 three other genetically related isozymes, esterase 2, esterase 7 and esterase 9, with respect to some physical and catalytic properties.