Studies on detergent released choline acetyltransferase from membrane fractions of rat and human brain

Gordon Bruce, Louis B. Hersh

Research output: Contribution to journalArticle

7 Scopus citations

Abstract

The relationship between soluble and membrane choline acetyltransferase (ChAT) was studied. Differential solubilization of rat and human brain yielded ChAT in the soluble and membrane fractions. The addition of 1% Triton X-100 to membrane fractions resulted in a release of ChAT. A comparable release of lactate dehydrogenase was also observed. The Triton released ChAT and soluble ChAT from rat and human brain were efficiently purified by immuno-affinity chromatography. A single molecular weight of 68,000 was observed for both forms of rat and human brain ChAT. Epitope maps produced from both forms of human brain ChAT were identical. It is concluded that Triton release ChAT is identical to soluble ChAT and simply represents occluded soluble ChAT.

Original languageEnglish (US)
Pages (from-to)1059-1066
Number of pages8
JournalNeurochemical Research
Volume12
Issue number12
DOIs
StatePublished - Dec 1 1987

Keywords

  • Choline acetyltransferase
  • brain
  • detergent solubilization
  • membranes

ASJC Scopus subject areas

  • Biochemistry
  • Cellular and Molecular Neuroscience

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