Irreversible thermal denaturation of Torpedo californica acetylcholinesterase
Thermal denaturation of Torpedo californica acetylcholinesterase, a disulfide‐linked homodimer with 537 amino acids in each subunit, was studied by differential scanning calorimetry. It displays a single calorimetric peak that is completely irreversible, the shape and temperature maximum depending o...
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| Published in | Protein science Vol. 4; no. 11; pp. 2349 - 2357 |
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| Main Authors | , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Bristol
Cold Spring Harbor Laboratory Press
01.11.1995
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| Online Access | Get full text |
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| Abstract | Thermal denaturation of Torpedo californica acetylcholinesterase, a disulfide‐linked homodimer with 537 amino acids in each subunit, was studied by differential scanning calorimetry. It displays a single calorimetric peak that is completely irreversible, the shape and temperature maximum depending on the scan rate. Thus, thermal denaturation of acetylcholinesterase is an irreversible process, under kinetic control, which is described well by the two‐state kinetic scheme N → D, with activation energy 131 ± 8 kcal/mol. Analysis of the kinetics of denaturation in the thermal transition temperature range, by monitoring loss of enzymic activity, yields activation energy of 121 ± 20 kcal/mol, similar to the value obtained by differential scanning calorimetry. Thermally denatured acetylcholinesterase displays spectroscopic characteristics typical of a molten globule state, similar to those of partially unfolded enzyme obtained by modification with thiol‐specific reagents. Evidence is presented that the partially unfolded states produced by the two different treatments are thermodynamically favored relative to the native state. |
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| AbstractList | Abstract
Thermal denaturation of
Torpedo californica
acetylcholinesterase, a disulfide‐linked homodimer with 537 amino acids in each subunit, was studied by differential scanning calorimetry. It displays a single calorimetric peak that is completely irreversible, the shape and temperature maximum depending on the scan rate. Thus, thermal denaturation of acetylcholinesterase is an irreversible process, under kinetic control, which is described well by the two‐state kinetic scheme N → D, with activation energy 131 ± 8 kcal/mol. Analysis of the kinetics of denaturation in the thermal transition temperature range, by monitoring loss of enzymic activity, yields activation energy of 121 ± 20 kcal/mol, similar to the value obtained by differential scanning calorimetry. Thermally denatured acetylcholinesterase displays spectroscopic characteristics typical of a molten globule state, similar to those of partially unfolded enzyme obtained by modification with thiol‐specific reagents. Evidence is presented that the partially unfolded states produced by the two different treatments are thermodynamically favored relative to the native state. Thermal denaturation of Torpedo californica acetylcholinesterase, a disulfide‐linked homodimer with 537 amino acids in each subunit, was studied by differential scanning calorimetry. It displays a single calorimetric peak that is completely irreversible, the shape and temperature maximum depending on the scan rate. Thus, thermal denaturation of acetylcholinesterase is an irreversible process, under kinetic control, which is described well by the two‐state kinetic scheme N → D, with activation energy 131 ± 8 kcal/mol. Analysis of the kinetics of denaturation in the thermal transition temperature range, by monitoring loss of enzymic activity, yields activation energy of 121 ± 20 kcal/mol, similar to the value obtained by differential scanning calorimetry. Thermally denatured acetylcholinesterase displays spectroscopic characteristics typical of a molten globule state, similar to those of partially unfolded enzyme obtained by modification with thiol‐specific reagents. Evidence is presented that the partially unfolded states produced by the two different treatments are thermodynamically favored relative to the native state. Thermal denaturation of Torpedo californica acetylcholinesterase, a disulfide-linked homodimer with 537 amino acids in each subunit, was studied by differential scanning calorimetry. It displays a single calorimetric peak that is completely irreversible, the shape and temperature maximum depending on the scan rate. Thus, thermal denaturation of acetylcholinesterase is an irreversible process, under kinetic control, which is described well by the two-state kinetic scheme N-->D, with activation energy 131 +/- 8 kcal/mol. Analysis of the kinetics of denaturation in the thermal transition temperature range, by monitoring loss of enzymic activity, yields activation energy of 121 +/- 20 kcal/mol, similar to the value obtained by differential scanning calorimetry. Thermally denatured acetylcholinesterase displays spectroscopic characteristics typical of a molten globule state, similar to those of partially unfolded enzyme obtained by modification with thiol-specific reagents. Evidence is presented that the partially unfolded states produced by the two different treatments are thermodynamically favored relative to the native state. Thermal denaturation of Torpedo californica acetylcholinesterase, a disulfide-linked homodimer with 537 amino acids in each subunit, was studied by differential scanning calorimetry. It displays a single calorimetric peak that is completely irreversible, the shape and temperature maximum depending on the scan rate. Thus, thermal denaturation of acetylcholinesterase is an irreversible process, under kinetic control, which is described well by the two-state kinetic scheme N-->D, with activation energy 131 +/- 8 kcal/mol. Analysis of the kinetics of denaturation in the thermal transition temperature range, by monitoring loss of enzymic activity, yields activation energy of 121 +/- 20 kcal/mol, similar to the value obtained by differential scanning calorimetry. Thermally denatured acetylcholinesterase displays spectroscopic characteristics typical of a molten globule state, similar to those of partially unfolded enzyme obtained by modification with thiol-specific reagents. Evidence is presented that the partially unfolded states produced by the two different treatments are thermodynamically favored relative to the native state. |
| Author | Kreimer, David I. Shnyrov, Valery L. Silman, Israel Villar, Enrique Weiner, Lev |
| AuthorAffiliation | Department of Neurobiology, Weizmann Institute of Science, Rehovot, Israel |
| AuthorAffiliation_xml | – name: Department of Neurobiology, Weizmann Institute of Science, Rehovot, Israel |
| Author_xml | – sequence: 1 givenname: David I. surname: Kreimer fullname: Kreimer, David I. – sequence: 2 givenname: Valery L. surname: Shnyrov fullname: Shnyrov, Valery L. – sequence: 3 givenname: Enrique surname: Villar fullname: Villar, Enrique – sequence: 4 givenname: Israel surname: Silman fullname: Silman, Israel – sequence: 5 givenname: Lev surname: Weiner fullname: Weiner, Lev email: cilev@weizmann.weizmann.ac.il |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/8563632$$D View this record in MEDLINE/PubMed |
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| Copyright | Copyright © 1995 The Protein Society |
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| Snippet | Thermal denaturation of Torpedo californica acetylcholinesterase, a disulfide‐linked homodimer with 537 amino acids in each subunit, was studied by... Thermal denaturation of Torpedo californica acetylcholinesterase, a disulfide-linked homodimer with 537 amino acids in each subunit, was studied by... Abstract Thermal denaturation of Torpedo californica acetylcholinesterase, a disulfide‐linked homodimer with 537 amino acids in each subunit, was studied by... |
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| SubjectTerms | acetylcholinesterase Acetylcholinesterase - chemistry Animals Calorimetry, Differential Scanning differential scanning calorimetry Disulfides - chemistry Electrophoresis, Polyacrylamide Gel Guanidine Guanidines Hot Temperature irreversible denaturation Kinetics molten globule Protein Denaturation Spectrometry, Fluorescence Sulfhydryl Compounds - chemistry Thermodynamics thiol‐disulfide exchange Torpedo two‐state kinetic model |
| Title | Irreversible thermal denaturation of Torpedo californica acetylcholinesterase |
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