Identification of discrete disulfide-linked oligomers which distinguish 18 S from 14 S acetylcholinesterase

William F X McCann, Terrone L. Rosenberry

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

Acetylcholinesterase (EC 3.1.1.7) purified by affinity chromatography from 1.0 m ionic strength extracts of electric organ from the eel Electrophorus electricus consists of a mixture of 18 and 14 S enzyme forms. When examined by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate without exposure to disulfide reducing agents, these purified preparations show two major high molecular weight bands (>300,000), labeled oligomers A and B, in addition to a major band corresponding to catalytic subunit dimers (150,000 Mr). All these major bands reflect intersubunit disulfide bonding. The 18 and 14 S forms in purified preparations were separated by extensive sucrose gradient centrifugation. Gel analyses of the isolated 18 and 14 S pools indicated that the larger oligomer A derives from the 18 S pool, while oligomer B is found primarily in the 14 S pool. These observations support a previous model for 18 S acetylcholinesterase (T. L. Rosenberry and J. M. Richardson (1977) Biochemistry, in press) which considers this molecule to consist of one oligomer A unit, composed of three pairs of catalytic subunits disulfide-bonded to a collagen-like tail structure, and three catalytic subunit dimers. Proteolytic cleavage of the tail structure in the 18 S form can occur to release an 11 S enzyme tetramer containing a residual tail fragment and to leave a 14 S form. We propose this 14 S form to consist of one oligomer B unit, composed of two pairs of catalytic subunits disulfide-bonded to the remaining tail structure, and two catalytic subunit dimers.

Original languageEnglish (US)
Pages (from-to)347-352
Number of pages6
JournalArchives of Biochemistry and Biophysics
Volume183
Issue number1
DOIs
StatePublished - 1977
Externally publishedYes

Fingerprint

Acetylcholinesterase
Oligomers
Disulfides
Catalytic Domain
Tail
Electrophorus
Dimers
Electric Organ
Affinity chromatography
Biochemistry
Centrifugation
Reducing Agents
Enzymes
Ionic strength
Electrophoresis
Affinity Chromatography
Sodium Dodecyl Sulfate
Osmolar Concentration
Sucrose
Polyacrylamide Gel Electrophoresis

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Identification of discrete disulfide-linked oligomers which distinguish 18 S from 14 S acetylcholinesterase. / McCann, William F X; Rosenberry, Terrone L.

In: Archives of Biochemistry and Biophysics, Vol. 183, No. 1, 1977, p. 347-352.

Research output: Contribution to journalArticle

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