Isolation of juvenile hormone esterase and its partial cDNA clone from the beetle, Tenebrio molitor

被引：18

作者：

Thomas, BA ^{[1
]}

Hinton, AC ^{[1
]}

Moskowitz, H ^{[1
]}

Severson, TF ^{[1
]}

Hammock, BD ^{[1
]}

机构：

[1] Univ Calif Davis, Dept Entomol, Davis, CA 95616 USA

来源：

INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY | 2000年 / 30卷 / 07期

关键词：

esterase; affinity chromatography; juvenile hormones; insects; hormones; Tenebrio molitor;

D O I：

10.1016/S0965-1748(00)00020-5

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Juvenile hormone esterase (JHE) plays an essential role in insect development. It is partially responsible for the clearance of juvenile hormone (JH) which regulates various aspects of insect development and reproduction. Because of its role in regulating JH titer, this enzyme has been targeted for development of biologically-based insecticides. JHE was partially purified from the beetle, Tenebrio molitor, using a transition state analog as the affinity ligand. Two forms of JHE were characterized by activity analysis, isoelectric focusing, two-dimensional SDS-PAGE and N-terminal sequence analysis. The esterase is associated with two proteins of sizes 71 and 150 kDa, both of which are active on JH III. A partial cDNA clone for the enzyme was isolated based on the sequence of N-terminal and internal peptides. Its sequence indicates that JHE from T. molitor and Heliothis virescens may have a common origin. (C) 2000 Published by Elsevier Science Ltd. All rights reserved.

引用

页码：529 / 540

页数：12

共 39 条

[1] APPARENT MULTIPLE CATALYTIC SITES INVOLVED IN THE ESTER HYDROLYSIS OF JUVENILE HORMONES BY THE HEMOLYMPH AND BY AN AFFINITY-PURIFIED ESTERASE FROM MANDUCA-SEXTA JOHANSSON (LEPIDOPTERA, SPHINGIDAE) [J].