Abstract
Four esterase isozymes hydrolyzing α-naphthyl acetate (α-NA) were detected screening whole body homogenates of larvae and adults of Ips typographus by electrophoresis. Two of the four isozymes (isozymes 3 and 4) were not detected by α-NA staining in the pupal stage, but topical application of juvenile hormone III (JH III) on the pupa induced these isozymes. The JH esterase (JHE) activity on the gel was associated with the proteins of isozyme 2. The compounds OTFP, PTFP, and DFP inhibited this catalytic activity of isozyme 2 on the gel at low concentrations, whereas the proteins of isozyme 3 and 4 were affected only at higher concentrations. A quantitative developmental study was performed to characterize which of the esterases hydrolyzed JH III, using a putative surrogate substrate for JH (HEXTAT) and α-NA. The I50 of several esterase inhibitors and the JH metabolites were also defined. All findings supported the results that a protein associated with isozyme 2 is catabolizing JH and that isozymes 3 and 4 are the main contributors to the general esterase activity on α-NA. The JHE from Tenebrio molitor was purified by affinity chromatography. Although the recovery was low, an analytical isoelectric focusing gel showed that the JHE activity of the purified enzyme T. molitor cochromatographed at the same pl as the JHE activity of I. typographus.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 203-221 |
| Number of pages | 19 |
| Journal | Archives of Insect Biochemistry and Physiology |
| Volume | 34 |
| Issue number | 2 |
| State | Published - 1997 |
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Keywords
- Developmental profile
- Ips typographus
- Juvenile hormone esterase
- Tenebrio molitor
ASJC Scopus subject areas
- Insect Science
- Biochemistry, Genetics and Molecular Biology(all)
- Physiology
- Physiology (medical)
Cite this
Characterization of the esterase isozymes of Ips typographus (Coleoptera, Scolytidae). / Stauffer, Christian; Shiotsuki, Takahiro; Chan, William; Hammock, Bruce D.
In: Archives of Insect Biochemistry and Physiology, Vol. 34, No. 2, 1997, p. 203-221.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Characterization of the esterase isozymes of Ips typographus (Coleoptera, Scolytidae)
AU - Stauffer, Christian
AU - Shiotsuki, Takahiro
AU - Chan, William
AU - Hammock, Bruce D.
PY - 1997
Y1 - 1997
N2 - Four esterase isozymes hydrolyzing α-naphthyl acetate (α-NA) were detected screening whole body homogenates of larvae and adults of Ips typographus by electrophoresis. Two of the four isozymes (isozymes 3 and 4) were not detected by α-NA staining in the pupal stage, but topical application of juvenile hormone III (JH III) on the pupa induced these isozymes. The JH esterase (JHE) activity on the gel was associated with the proteins of isozyme 2. The compounds OTFP, PTFP, and DFP inhibited this catalytic activity of isozyme 2 on the gel at low concentrations, whereas the proteins of isozyme 3 and 4 were affected only at higher concentrations. A quantitative developmental study was performed to characterize which of the esterases hydrolyzed JH III, using a putative surrogate substrate for JH (HEXTAT) and α-NA. The I50 of several esterase inhibitors and the JH metabolites were also defined. All findings supported the results that a protein associated with isozyme 2 is catabolizing JH and that isozymes 3 and 4 are the main contributors to the general esterase activity on α-NA. The JHE from Tenebrio molitor was purified by affinity chromatography. Although the recovery was low, an analytical isoelectric focusing gel showed that the JHE activity of the purified enzyme T. molitor cochromatographed at the same pl as the JHE activity of I. typographus.
AB - Four esterase isozymes hydrolyzing α-naphthyl acetate (α-NA) were detected screening whole body homogenates of larvae and adults of Ips typographus by electrophoresis. Two of the four isozymes (isozymes 3 and 4) were not detected by α-NA staining in the pupal stage, but topical application of juvenile hormone III (JH III) on the pupa induced these isozymes. The JH esterase (JHE) activity on the gel was associated with the proteins of isozyme 2. The compounds OTFP, PTFP, and DFP inhibited this catalytic activity of isozyme 2 on the gel at low concentrations, whereas the proteins of isozyme 3 and 4 were affected only at higher concentrations. A quantitative developmental study was performed to characterize which of the esterases hydrolyzed JH III, using a putative surrogate substrate for JH (HEXTAT) and α-NA. The I50 of several esterase inhibitors and the JH metabolites were also defined. All findings supported the results that a protein associated with isozyme 2 is catabolizing JH and that isozymes 3 and 4 are the main contributors to the general esterase activity on α-NA. The JHE from Tenebrio molitor was purified by affinity chromatography. Although the recovery was low, an analytical isoelectric focusing gel showed that the JHE activity of the purified enzyme T. molitor cochromatographed at the same pl as the JHE activity of I. typographus.
KW - Developmental profile
KW - Ips typographus
KW - Juvenile hormone esterase
KW - Tenebrio molitor
UR - http://www.scopus.com/inward/record.url?scp=0000573321&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0000573321&partnerID=8YFLogxK
M3 - Article
AN - SCOPUS:0000573321
VL - 34
SP - 203
EP - 221
JO - Archives of Insect Biochemistry and Physiology
JF - Archives of Insect Biochemistry and Physiology
SN - 0739-4462
IS - 2
ER -