A comparison of the induced and naturally occurring juvenile hormone esterases from last instar larvae of Trichoplusia ni

Thomas C. Sparks, Bruce D. Hammock

Research output: Contribution to journalArticle

59 Citations (Scopus)

Abstract

During the last larval instar of Trichoplusia ni two naturally occurring peaks of juvenile hormone esterase activity are present. After a critical period, juvenile hormone esterase activity can be induced in normal and ligated larvae by the topical application of juvenile hormone or juvenoids. The natural and artificially induced juvenile hormone esterases are similarly inhibited by a selected group of organophosphate and carbamate inhibitors. Paraoxon and O-ethyl-S-phenyl phosphoramidothiolate displayed the best inhibition, both with an I50 of 1 × 10-6M, while several general esterase inhibitors, including diisopropyl phosphorofluoridate, had very little effect. The three groups of juvenile hormone esterases have similiar gel filtration patterns which are distinct from most of the α-naphthyl acetate esterase activity. The natural and artificially induced juvenile hormone esterases demonstrated identical migration patterns when analyzed by gel electrophoresis. Isoelectric focusing also resulted in essentially identical activity patterns and pI values for each of the three groups of juvenile hormone esterases. Both naturally occurring peaks of juvenile hormone esterase activity as well as an artificially induced peak of juvenile hormone esterase activity appear to be largely due to one enzyme, and within the limits of the techniques used, these esterases are identical. The juvenile hormone esterase activity is distinct from and more stable than the majority of the α-naphthyl acetate esterase activity in the haemolymph.

Original languageEnglish (US)
Pages (from-to)411-421
Number of pages11
JournalInsect Biochemistry
Volume9
Issue number4
DOIs
StatePublished - 1979

Fingerprint

juvenile hormone esterase
Trichoplusia ni
Larva
instars
larvae
esterases
Acetylesterase
Esterases
Gels
acetates
Paraoxon
paraoxon
Juvenile Hormones
juvenile hormone analogs
Carbamates
Organophosphates
Hemolymph
carbamates
topical application
isoelectric focusing

Keywords

  • gel electrophoresis
  • gel filtration
  • haemolymph proteins
  • inhibition
  • isoelectric focusing
  • Juvenile hormone esterase
  • phosphoramidothiolate
  • Trichoplusia ni
  • α-naphthyl acetate esterase

Cite this

A comparison of the induced and naturally occurring juvenile hormone esterases from last instar larvae of Trichoplusia ni. / Sparks, Thomas C.; Hammock, Bruce D.

In: Insect Biochemistry, Vol. 9, No. 4, 1979, p. 411-421.

Research output: Contribution to journalArticle

@article{2edcabeeb83944fb80476a406d0b6c3f,
title = "A comparison of the induced and naturally occurring juvenile hormone esterases from last instar larvae of Trichoplusia ni",
abstract = "During the last larval instar of Trichoplusia ni two naturally occurring peaks of juvenile hormone esterase activity are present. After a critical period, juvenile hormone esterase activity can be induced in normal and ligated larvae by the topical application of juvenile hormone or juvenoids. The natural and artificially induced juvenile hormone esterases are similarly inhibited by a selected group of organophosphate and carbamate inhibitors. Paraoxon and O-ethyl-S-phenyl phosphoramidothiolate displayed the best inhibition, both with an I50 of 1 × 10-6M, while several general esterase inhibitors, including diisopropyl phosphorofluoridate, had very little effect. The three groups of juvenile hormone esterases have similiar gel filtration patterns which are distinct from most of the α-naphthyl acetate esterase activity. The natural and artificially induced juvenile hormone esterases demonstrated identical migration patterns when analyzed by gel electrophoresis. Isoelectric focusing also resulted in essentially identical activity patterns and pI values for each of the three groups of juvenile hormone esterases. Both naturally occurring peaks of juvenile hormone esterase activity as well as an artificially induced peak of juvenile hormone esterase activity appear to be largely due to one enzyme, and within the limits of the techniques used, these esterases are identical. The juvenile hormone esterase activity is distinct from and more stable than the majority of the α-naphthyl acetate esterase activity in the haemolymph.",
keywords = "gel electrophoresis, gel filtration, haemolymph proteins, inhibition, isoelectric focusing, Juvenile hormone esterase, phosphoramidothiolate, Trichoplusia ni, α-naphthyl acetate esterase",
author = "Sparks, {Thomas C.} and Hammock, {Bruce D.}",
year = "1979",
doi = "10.1016/0020-1790(79)90091-X",
language = "English (US)",
volume = "9",
pages = "411--421",
journal = "Insect Biochemistry and Molecular Biology",
issn = "0965-1748",
publisher = "Elsevier Limited",
number = "4",

}

TY - JOUR

T1 - A comparison of the induced and naturally occurring juvenile hormone esterases from last instar larvae of Trichoplusia ni

AU - Sparks, Thomas C.

AU - Hammock, Bruce D.

PY - 1979

Y1 - 1979

N2 - During the last larval instar of Trichoplusia ni two naturally occurring peaks of juvenile hormone esterase activity are present. After a critical period, juvenile hormone esterase activity can be induced in normal and ligated larvae by the topical application of juvenile hormone or juvenoids. The natural and artificially induced juvenile hormone esterases are similarly inhibited by a selected group of organophosphate and carbamate inhibitors. Paraoxon and O-ethyl-S-phenyl phosphoramidothiolate displayed the best inhibition, both with an I50 of 1 × 10-6M, while several general esterase inhibitors, including diisopropyl phosphorofluoridate, had very little effect. The three groups of juvenile hormone esterases have similiar gel filtration patterns which are distinct from most of the α-naphthyl acetate esterase activity. The natural and artificially induced juvenile hormone esterases demonstrated identical migration patterns when analyzed by gel electrophoresis. Isoelectric focusing also resulted in essentially identical activity patterns and pI values for each of the three groups of juvenile hormone esterases. Both naturally occurring peaks of juvenile hormone esterase activity as well as an artificially induced peak of juvenile hormone esterase activity appear to be largely due to one enzyme, and within the limits of the techniques used, these esterases are identical. The juvenile hormone esterase activity is distinct from and more stable than the majority of the α-naphthyl acetate esterase activity in the haemolymph.

AB - During the last larval instar of Trichoplusia ni two naturally occurring peaks of juvenile hormone esterase activity are present. After a critical period, juvenile hormone esterase activity can be induced in normal and ligated larvae by the topical application of juvenile hormone or juvenoids. The natural and artificially induced juvenile hormone esterases are similarly inhibited by a selected group of organophosphate and carbamate inhibitors. Paraoxon and O-ethyl-S-phenyl phosphoramidothiolate displayed the best inhibition, both with an I50 of 1 × 10-6M, while several general esterase inhibitors, including diisopropyl phosphorofluoridate, had very little effect. The three groups of juvenile hormone esterases have similiar gel filtration patterns which are distinct from most of the α-naphthyl acetate esterase activity. The natural and artificially induced juvenile hormone esterases demonstrated identical migration patterns when analyzed by gel electrophoresis. Isoelectric focusing also resulted in essentially identical activity patterns and pI values for each of the three groups of juvenile hormone esterases. Both naturally occurring peaks of juvenile hormone esterase activity as well as an artificially induced peak of juvenile hormone esterase activity appear to be largely due to one enzyme, and within the limits of the techniques used, these esterases are identical. The juvenile hormone esterase activity is distinct from and more stable than the majority of the α-naphthyl acetate esterase activity in the haemolymph.

KW - gel electrophoresis

KW - gel filtration

KW - haemolymph proteins

KW - inhibition

KW - isoelectric focusing

KW - Juvenile hormone esterase

KW - phosphoramidothiolate

KW - Trichoplusia ni

KW - α-naphthyl acetate esterase

UR - http://www.scopus.com/inward/record.url?scp=0003080374&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0003080374&partnerID=8YFLogxK

U2 - 10.1016/0020-1790(79)90091-X

DO - 10.1016/0020-1790(79)90091-X

M3 - Article

VL - 9

SP - 411

EP - 421

JO - Insect Biochemistry and Molecular Biology

JF - Insect Biochemistry and Molecular Biology

SN - 0965-1748

IS - 4

ER -