Thermal inactivation of the molecular forms of acetylcholinesterase and butyrylcholinesterase

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Abstract

To compare acetylcholinesterase (acetylcholine acetylhydrolase, EC 3.1.1.7) and butyrylcholinesterase (acylcholine acylhydrolase, EC 3.1.1.8), we utilized the physical parameter of thermolability. In serum or muscle extracts from mouse and rat, butyryclholinesterase was inactivated as a unimodal function of temperature. Inactivation began at 51°C and was complete at 54-57°C (depending upon time of incubation). Acetylcholinesterase was inactivated in two stages. A 60% decrease in activity from 42 to 48°C was followed by a plateau. The second stage of inactivation began at 51°C and was complete at 57-60°C (depending upon time of incubation). Sucrose density gradients revealed that the partial loss of acetylcholinesterase activity at 48°C was due to inactivation of the monomeric 4 S enzyme, which was the most thermolabile molecular form in each tissue examined. When heated after isolation on density gradients, most of the forms of acetylcholinesterase and butyrylcholinesterase lost activityas a single exponential function of time. The monomers of both enzymes were inactivated fastest. Inactivation of the larger forms was slower and required higher temperatures. Tetrameric 10 S acetylcholinesterase was unique in following a time course that could only be fitted by a double exponential equation (i.e., when this form was heated to 55°C, almost 60% of the activity showed a short half-life while the remainder showed a long half-life). This behavior did not reflect differences in the thermolability of soluble and membrane-derived tetramers.

Original languageEnglish (US)
Pages (from-to)509-516
Number of pages8
JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Volume742
Issue number3
DOIs
StatePublished - Feb 15 1983

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Butyrylcholinesterase
Acetylcholinesterase
Hot Temperature
Cholinesterases
Half-Life
Temperature
Exponential functions
Enzymes
Sucrose
Muscle
Rats
Monomers
Tissue
Membranes
Muscles
Serum

Keywords

  • (Rodent)
  • Acetylcholinesterase
  • Butyrylcholinesterase,' Heat stability
  • Monomeric form

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology
  • Structural Biology
  • Medicine(all)

Cite this

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title = "Thermal inactivation of the molecular forms of acetylcholinesterase and butyrylcholinesterase",
abstract = "To compare acetylcholinesterase (acetylcholine acetylhydrolase, EC 3.1.1.7) and butyrylcholinesterase (acylcholine acylhydrolase, EC 3.1.1.8), we utilized the physical parameter of thermolability. In serum or muscle extracts from mouse and rat, butyryclholinesterase was inactivated as a unimodal function of temperature. Inactivation began at 51°C and was complete at 54-57°C (depending upon time of incubation). Acetylcholinesterase was inactivated in two stages. A 60{\%} decrease in activity from 42 to 48°C was followed by a plateau. The second stage of inactivation began at 51°C and was complete at 57-60°C (depending upon time of incubation). Sucrose density gradients revealed that the partial loss of acetylcholinesterase activity at 48°C was due to inactivation of the monomeric 4 S enzyme, which was the most thermolabile molecular form in each tissue examined. When heated after isolation on density gradients, most of the forms of acetylcholinesterase and butyrylcholinesterase lost activityas a single exponential function of time. The monomers of both enzymes were inactivated fastest. Inactivation of the larger forms was slower and required higher temperatures. Tetrameric 10 S acetylcholinesterase was unique in following a time course that could only be fitted by a double exponential equation (i.e., when this form was heated to 55°C, almost 60{\%} of the activity showed a short half-life while the remainder showed a long half-life). This behavior did not reflect differences in the thermolability of soluble and membrane-derived tetramers.",
keywords = "(Rodent), Acetylcholinesterase, Butyrylcholinesterase,' Heat stability, Monomeric form",
author = "Edwards, {J. A.} and Brimijoin, {William Stephen}",
year = "1983",
month = "2",
day = "15",
doi = "10.1016/0167-4838(83)90268-6",
language = "English (US)",
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pages = "509--516",
journal = "Biochimica et Biophysica Acta - Proteins and Proteomics",
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TY - JOUR

T1 - Thermal inactivation of the molecular forms of acetylcholinesterase and butyrylcholinesterase

AU - Edwards, J. A.

AU - Brimijoin, William Stephen

PY - 1983/2/15

Y1 - 1983/2/15

N2 - To compare acetylcholinesterase (acetylcholine acetylhydrolase, EC 3.1.1.7) and butyrylcholinesterase (acylcholine acylhydrolase, EC 3.1.1.8), we utilized the physical parameter of thermolability. In serum or muscle extracts from mouse and rat, butyryclholinesterase was inactivated as a unimodal function of temperature. Inactivation began at 51°C and was complete at 54-57°C (depending upon time of incubation). Acetylcholinesterase was inactivated in two stages. A 60% decrease in activity from 42 to 48°C was followed by a plateau. The second stage of inactivation began at 51°C and was complete at 57-60°C (depending upon time of incubation). Sucrose density gradients revealed that the partial loss of acetylcholinesterase activity at 48°C was due to inactivation of the monomeric 4 S enzyme, which was the most thermolabile molecular form in each tissue examined. When heated after isolation on density gradients, most of the forms of acetylcholinesterase and butyrylcholinesterase lost activityas a single exponential function of time. The monomers of both enzymes were inactivated fastest. Inactivation of the larger forms was slower and required higher temperatures. Tetrameric 10 S acetylcholinesterase was unique in following a time course that could only be fitted by a double exponential equation (i.e., when this form was heated to 55°C, almost 60% of the activity showed a short half-life while the remainder showed a long half-life). This behavior did not reflect differences in the thermolability of soluble and membrane-derived tetramers.

AB - To compare acetylcholinesterase (acetylcholine acetylhydrolase, EC 3.1.1.7) and butyrylcholinesterase (acylcholine acylhydrolase, EC 3.1.1.8), we utilized the physical parameter of thermolability. In serum or muscle extracts from mouse and rat, butyryclholinesterase was inactivated as a unimodal function of temperature. Inactivation began at 51°C and was complete at 54-57°C (depending upon time of incubation). Acetylcholinesterase was inactivated in two stages. A 60% decrease in activity from 42 to 48°C was followed by a plateau. The second stage of inactivation began at 51°C and was complete at 57-60°C (depending upon time of incubation). Sucrose density gradients revealed that the partial loss of acetylcholinesterase activity at 48°C was due to inactivation of the monomeric 4 S enzyme, which was the most thermolabile molecular form in each tissue examined. When heated after isolation on density gradients, most of the forms of acetylcholinesterase and butyrylcholinesterase lost activityas a single exponential function of time. The monomers of both enzymes were inactivated fastest. Inactivation of the larger forms was slower and required higher temperatures. Tetrameric 10 S acetylcholinesterase was unique in following a time course that could only be fitted by a double exponential equation (i.e., when this form was heated to 55°C, almost 60% of the activity showed a short half-life while the remainder showed a long half-life). This behavior did not reflect differences in the thermolability of soluble and membrane-derived tetramers.

KW - (Rodent)

KW - Acetylcholinesterase

KW - Butyrylcholinesterase,' Heat stability

KW - Monomeric form

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U2 - 10.1016/0167-4838(83)90268-6

DO - 10.1016/0167-4838(83)90268-6

M3 - Article

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AN - SCOPUS:0020679804

VL - 742

SP - 509

EP - 516

JO - Biochimica et Biophysica Acta - Proteins and Proteomics

JF - Biochimica et Biophysica Acta - Proteins and Proteomics

SN - 1570-9639

IS - 3

ER -