Structure of 11S acetylcholinesterase. Subunit composition

Terrone L. Rosenberry, Yueh T. Chen, Ernest Bock

Research output: Contribution to journalArticle

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Abstract

The subunit compositions of several 11S acetylcholinesterase (EC 3.1.1.7) preparations from the electric eel were investigated. Data from polyacrylamide gel electrophoresis in 1% sodium dodecyl sulfate and gel exclusion chromatography in 6 M guanidine hydrochloride indicated that the active enzyme is a tetramer composed of subunits with molecular weights of 70,000. From analyses of 32P-phosphorylation patterns and cyanogen bromide fragment compositions, the subunits were shown to contain one active site each and to be identical within the limits imposed by these techniques, except for a variability in manifesting two sites of cleavage, probably caused by proteolytic or glycolytic agents. One cleavage occurs at a site A and splits the intact subunit (I) into a major fragment (II) of 50,000 molecular weight and a minor fragment (III) of 20,000-22,000 molecular weight. A second cleavage at a site B generates a second minor fragment (IV), with a molecular weight of 18,000-20,000, from III. In the absence of disulfide reduction these cleavages did not appear to result in the release of measurable polypeptides from the subunit structures. In the native enzyme both cleaved and intact subunits appear to exist as subunit dimers with a covalent intersubunit linkage which involves disulfide bonding. Hence the subunits in the native tetramer are arranged as a dimer of dimers ((α)2)2, where α is either the cleaved or intact subunit containing the catalytic site.

Original languageEnglish (US)
Pages (from-to)3068-3079
Number of pages12
JournalBiochemistry
Volume13
Issue number15
StatePublished - 1974
Externally publishedYes

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Acetylcholinesterase
Molecular Weight
Molecular weight
Dimers
Chemical analysis
Disulfides
Gel Chromatography
Catalytic Domain
Electrophorus
Cyanogen Bromide
Phosphorylation
Guanidine
Enzymes
Chromatography
Electrophoresis
Sodium Dodecyl Sulfate
Polyacrylamide Gel Electrophoresis
Gels
Peptides

ASJC Scopus subject areas

  • Biochemistry

Cite this

Rosenberry, T. L., Chen, Y. T., & Bock, E. (1974). Structure of 11S acetylcholinesterase. Subunit composition. Biochemistry, 13(15), 3068-3079.

Structure of 11S acetylcholinesterase. Subunit composition. / Rosenberry, Terrone L.; Chen, Yueh T.; Bock, Ernest.

In: Biochemistry, Vol. 13, No. 15, 1974, p. 3068-3079.

Research output: Contribution to journalArticle

Rosenberry, TL, Chen, YT & Bock, E 1974, 'Structure of 11S acetylcholinesterase. Subunit composition', Biochemistry, vol. 13, no. 15, pp. 3068-3079.
Rosenberry TL, Chen YT, Bock E. Structure of 11S acetylcholinesterase. Subunit composition. Biochemistry. 1974;13(15):3068-3079.
Rosenberry, Terrone L. ; Chen, Yueh T. ; Bock, Ernest. / Structure of 11S acetylcholinesterase. Subunit composition. In: Biochemistry. 1974 ; Vol. 13, No. 15. pp. 3068-3079.
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