Literature DB >> 4821394

The molecular form of acetylcholinesterase as determined by irradiation inactivation.

S R Levinson, J C Ellory.   

Abstract

The molecular size of acetylcholinesterase (EC 3.1.1.7) from the electric organ of Electrophorus electricus and erythrocyte ;ghosts' was estimated in both membrane-bound and purified preparations by irradiation inactivation. Results suggest that the form of the enzyme in the membrane is a monomer of molecular weight approx. 75000 and that multiple forms of the enzyme observed in solubilized preparations are aggregates of this monomer.

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Year:  1974        PMID： 4821394      PMCID： PMC1166090          DOI： 10.1042/bj1370123

Source DB:  PubMed          Journal:  Biochem J        ISSN： 0264-6021            Impact factor:   3.857


  12 in total

1.  The subunit molecular weight of acetylcholinesterase.

Authors:  David B. Millar; Melba A. Grafius
Journal:  FEBS Lett       Date:  1970-12-23       Impact factor: 4.124

2.  A simplified procedure for for the partial purification of acetylcholinesterase from electric tissue.

Authors:  H C LAWLER
Journal:  J Biol Chem       Date:  1959-04       Impact factor: 5.157

3.  Suramin: a potent ATPase inhibitor which acts on the inside surface of the sodium pump.

Authors:  P A Fortes; J C Ellory; V L Lew
Journal:  Biochim Biophys Acta       Date:  1973-08-22

4.  Molecular size of the tetrodotoxin binding site estimated by irradiation inactivation.

Authors:  S R Levinson; J C Ellory
Journal:  Nat New Biol       Date:  1973-09-26

5.  Multiple forms of acetylcholinesterase from pig brain.

Authors:  C H McIntosh; D T Plummer
Journal:  Biochem J       Date:  1973-08       Impact factor: 3.857

6.  The release and molecular state of mammalian brain acetylcholinesterase.

Authors:  E G Hollunger; B H Niklasson
Journal:  J Neurochem       Date:  1973-03       Impact factor: 5.372

7.  Enzymatically active half-monomers of acetylcholinesterase.

Authors:  D B Millar; M A Grafius; D A Palmer
Journal:  Eur J Biochem       Date:  1973-09-03

8.  Membrane enzyme systems. Molecular size determinations by radiation inactivation.

Authors:  G R Kepner; R I Macey
Journal:  Biochim Biophys Acta       Date:  1968-09-17

9.  On the subunit structure of acetylcholinesterase.

Authors:  H C Froede; I B Wilson
Journal:  Isr J Med Sci       Date:  1970 Mar-Apr

10.  Mammalian brain acetylcholinesterase. Purification and properties.

Authors:  R L Jackson; M H Aprison
Journal:  J Neurochem       Date:  1966-12       Impact factor: 5.372
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  8 in total

1.  Analysis of the forms of acetylcholinesterase from adult mouse brain.

Authors:  E D Adamson; S E Ayers; Z A Deussen; C F Graham
Journal:  Biochem J       Date:  1975-05       Impact factor: 3.857

2.  Regulatory proteins (inhibitors or activators) affect estimates of Mr of enzymes and receptors by radiation inactivation. A theoretical model.

Authors:  M Potier; S Giroux
Journal:  Biochem J       Date:  1985-03-15       Impact factor: 3.857

3.  Functional lysosomal hydrolase size as determined by radiation inactivation analysis.

Authors:  G Dawson; J C Ellory
Journal:  Biochem J       Date:  1985-02-15       Impact factor: 3.857

4.  Molecular-size standards for use in radiation-inactivation studies on proteins.

Authors:  J H Nugent
Journal:  Biochem J       Date:  1986-10-15       Impact factor: 3.857

5.  Nucleoside transport in human erythrocytes. Apparent molecular weight of the nitrobenzylthioinosine-binding complex estimated by radiation-inactivation analysis.

Authors:  S M Jarvis; J D Young; J C Ellory
Journal:  Biochem J       Date:  1980-08-15       Impact factor: 3.857

6.  Studies of the acetylcholinesterase from houseflies (Musca domestica L.) resistant and susceptible to organophosphorus insecticides.

Authors:  A L Devonshire
Journal:  Biochem J       Date:  1975-08       Impact factor: 3.857

7.  Characterization of lipid-protein interactions in acetylcholinesterase lipoprotein extracted from bovine erythrocytes.

Authors:  G Beauregard; B D Roufogalis
Journal:  Biochem J       Date:  1979-04-01       Impact factor: 3.857

8.  Target size of neurotoxic esterase and acetylcholinesterase as determined by radiation inactivation.

Authors:  C D Carrington; D J Fluke; M B Abou-Donia
Journal:  Biochem J       Date:  1985-11-01       Impact factor: 3.857
  8 in total

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