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Acta Biochimica et Biophysica Sinica Advance Access originally published online on July 30, 2009
Acta Biochimica et Biophysica Sinica 2009 41(9):731-736; doi:10.1093/abbs/gmp061
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© The Author 2009. Published by ABBS Editorial Office in association with Oxford University Press on behalf of the Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences.

Baculo-expression and enzymatic characterization of CES7 esterase

Li Zhang1,2, Qiang Liu1,*, Yuchuan Zhou1,* and Yonglian Zhang1,3

1 Shanghai Key Laboratory for Molecular Andrology, State Key Laboratory of Molecular Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China
2 The Graduate School of Chinese Academy of Sciences, Beijing 100049, China
3 Shanghai Institute of Planned Parenthood Research, Shanghai 200032, China

* Correspondence address. Tel: +86-21-54921267; Fax: +86-21-54921011; E-mail: qliu{at}sibs.ac.cn (Q.L.); Tel: +86-21-54921153; Fax: +86-21-54921011; E-mail: zhouych{at}sibs.ac.cn (Y.Z.)


  Abstract

The male reproductive tracts in different species are characterized by similar patterns of male-dependent overexpression of carboxylesterases. This phenomenon indicates male sex-associated functions of these enzymes for spermatogenesis, sperm maturation, and sperm use. Recently, a novel epididymis-specific gene named Ces7 was cloned and characterized, which belongs to the carboxylesterase family. To study the functions of CES7 in sperm maturation and storage, CES7 recombinant protein was expressed in baculovirus system. The recombinant protein had carboxylesterase activity hydrolyzing cholesterol ester and choline ester. CES7 as carboxylesterase might be involved in ester hydrolysis, sperm maturation, and storage in male reproductive tract.

Keywords    esterase; carboxylesterase; baculo-expression

Received: April 17, 2009; Accepted: May 18, 2009
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