Determination and characterization of cholinesterases in localized tissues of the giant garden slugs Limax maximus (Linnaeus)

Isaac N Pessah, Phillip G. Sokolove

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

1. Evidence is presented for the presence of two types of cholinesterase in localized tissues of the terrestrial slug, Limax maximus, by use of substrates, inhibitors, and differential centrifugation. 2. An acetylcholine-type enzyme (AChE, EC 3.1.1.7) occurs in the circumoesophageal ganglia and muscular foot of the animal. It exhibits novel properties, including appreciable activity towards propionyl esters, lower sensitivity to inhibition by the AChE inhibitor BW284C51, and passes spontaneously (> 99%) into solution. 3. A second enzyme occurs in the hemolymph. It exhibits a substrate-activity profile characteristic of a non-specific propionylcholinesterase (PrChE, EC 3.1.1.8). 4. PrChE in Limax hemolymph (about 50% of the total activity) is associated with material pelletable in a 110,000 g spin presumed to be hemocyanin. 5. Progressive inhibition with iso-OMPA reveals that each enzyme is composed of two components. The AChE-type enzyme has a component, comprising 35% of the total activity, that is highly resistant to iso-OMPA inhibition. A similarly resistant component is absent in the hemolymph enzyme.

Original languageEnglish (US)
Pages (from-to)281-289
Number of pages9
JournalComparative Biochemistry and Physiology. Part C, Comparative
Volume74
Issue number2
DOIs
StatePublished - 1983
Externally publishedYes

Fingerprint

Gastropoda
Cholinesterases
Hemolymph
Tetraisopropylpyrophosphamide
Enzymes
Benzenaminium, 4,4'-(3-oxo-1,5-pentanediyl)bis(N,N-dimethyl-N-2-propenyl-), Dibromide
Hemocyanin
Centrifugation
Ganglia
Acetylcholine
Foot
Esters

ASJC Scopus subject areas

  • Immunology
  • Pharmacology

Cite this

@article{bb2a8c6ede214699a9837d96e90f6001,
title = "Determination and characterization of cholinesterases in localized tissues of the giant garden slugs Limax maximus (Linnaeus)",
abstract = "1. Evidence is presented for the presence of two types of cholinesterase in localized tissues of the terrestrial slug, Limax maximus, by use of substrates, inhibitors, and differential centrifugation. 2. An acetylcholine-type enzyme (AChE, EC 3.1.1.7) occurs in the circumoesophageal ganglia and muscular foot of the animal. It exhibits novel properties, including appreciable activity towards propionyl esters, lower sensitivity to inhibition by the AChE inhibitor BW284C51, and passes spontaneously (> 99{\%}) into solution. 3. A second enzyme occurs in the hemolymph. It exhibits a substrate-activity profile characteristic of a non-specific propionylcholinesterase (PrChE, EC 3.1.1.8). 4. PrChE in Limax hemolymph (about 50{\%} of the total activity) is associated with material pelletable in a 110,000 g spin presumed to be hemocyanin. 5. Progressive inhibition with iso-OMPA reveals that each enzyme is composed of two components. The AChE-type enzyme has a component, comprising 35{\%} of the total activity, that is highly resistant to iso-OMPA inhibition. A similarly resistant component is absent in the hemolymph enzyme.",
author = "Pessah, {Isaac N} and Sokolove, {Phillip G.}",
year = "1983",
doi = "10.1016/0742-8413(83)90102-0",
language = "English (US)",
volume = "74",
pages = "281--289",
journal = "Comparative biochemistry and physiology. C: Comparative pharmacology",
issn = "0742-8413",
publisher = "Elsevier BV",
number = "2",

}

TY - JOUR

T1 - Determination and characterization of cholinesterases in localized tissues of the giant garden slugs Limax maximus (Linnaeus)

AU - Pessah, Isaac N

AU - Sokolove, Phillip G.

PY - 1983

Y1 - 1983

N2 - 1. Evidence is presented for the presence of two types of cholinesterase in localized tissues of the terrestrial slug, Limax maximus, by use of substrates, inhibitors, and differential centrifugation. 2. An acetylcholine-type enzyme (AChE, EC 3.1.1.7) occurs in the circumoesophageal ganglia and muscular foot of the animal. It exhibits novel properties, including appreciable activity towards propionyl esters, lower sensitivity to inhibition by the AChE inhibitor BW284C51, and passes spontaneously (> 99%) into solution. 3. A second enzyme occurs in the hemolymph. It exhibits a substrate-activity profile characteristic of a non-specific propionylcholinesterase (PrChE, EC 3.1.1.8). 4. PrChE in Limax hemolymph (about 50% of the total activity) is associated with material pelletable in a 110,000 g spin presumed to be hemocyanin. 5. Progressive inhibition with iso-OMPA reveals that each enzyme is composed of two components. The AChE-type enzyme has a component, comprising 35% of the total activity, that is highly resistant to iso-OMPA inhibition. A similarly resistant component is absent in the hemolymph enzyme.

AB - 1. Evidence is presented for the presence of two types of cholinesterase in localized tissues of the terrestrial slug, Limax maximus, by use of substrates, inhibitors, and differential centrifugation. 2. An acetylcholine-type enzyme (AChE, EC 3.1.1.7) occurs in the circumoesophageal ganglia and muscular foot of the animal. It exhibits novel properties, including appreciable activity towards propionyl esters, lower sensitivity to inhibition by the AChE inhibitor BW284C51, and passes spontaneously (> 99%) into solution. 3. A second enzyme occurs in the hemolymph. It exhibits a substrate-activity profile characteristic of a non-specific propionylcholinesterase (PrChE, EC 3.1.1.8). 4. PrChE in Limax hemolymph (about 50% of the total activity) is associated with material pelletable in a 110,000 g spin presumed to be hemocyanin. 5. Progressive inhibition with iso-OMPA reveals that each enzyme is composed of two components. The AChE-type enzyme has a component, comprising 35% of the total activity, that is highly resistant to iso-OMPA inhibition. A similarly resistant component is absent in the hemolymph enzyme.

UR - http://www.scopus.com/inward/record.url?scp=0020600890&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0020600890&partnerID=8YFLogxK

U2 - 10.1016/0742-8413(83)90102-0

DO - 10.1016/0742-8413(83)90102-0

M3 - Article

AN - SCOPUS:0020600890

VL - 74

SP - 281

EP - 289

JO - Comparative biochemistry and physiology. C: Comparative pharmacology

JF - Comparative biochemistry and physiology. C: Comparative pharmacology

SN - 0742-8413

IS - 2

ER -