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 Citations (Scopus)

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 1987

Fingerprint

Choline O-Acetyltransferase
Detergents
Rats
Brain
Membranes
Affinity chromatography
Octoxynol
Affinity Chromatography
L-Lactate Dehydrogenase
Epitopes
Molecular Weight
Molecular weight

Keywords

  • brain
  • Choline acetyltransferase
  • detergent solubilization
  • membranes

ASJC Scopus subject areas

  • Biochemistry
  • Cellular and Molecular Neuroscience

Cite this

Studies on detergent released choline acetyltransferase from membrane fractions of rat and human brain. / Bruce, Gordon; Hersh, Louis B.

In: Neurochemical Research, Vol. 12, No. 12, 12.1987, p. 1059-1066.

Research output: Contribution to journalArticle

@article{eababb5bc0c44e7c8f1e60fdc5457682,
title = "Studies on detergent released choline acetyltransferase from membrane fractions of rat and human brain",
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.",
keywords = "brain, Choline acetyltransferase, detergent solubilization, membranes",
author = "Gordon Bruce and Hersh, {Louis B.}",
year = "1987",
month = "12",
doi = "10.1007/BF00971705",
language = "English (US)",
volume = "12",
pages = "1059--1066",
journal = "Neurochemical Research",
issn = "0364-3190",
publisher = "Springer New York",
number = "12",

}

TY - JOUR

T1 - Studies on detergent released choline acetyltransferase from membrane fractions of rat and human brain

AU - Bruce, Gordon

AU - Hersh, Louis B.

PY - 1987/12

Y1 - 1987/12

N2 - 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.

AB - 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.

KW - brain

KW - Choline acetyltransferase

KW - detergent solubilization

KW - membranes

UR - http://www.scopus.com/inward/record.url?scp=0023546742&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0023546742&partnerID=8YFLogxK

U2 - 10.1007/BF00971705

DO - 10.1007/BF00971705

M3 - Article

C2 - 2450285

AN - SCOPUS:0023546742

VL - 12

SP - 1059

EP - 1066

JO - Neurochemical Research

JF - Neurochemical Research

SN - 0364-3190

IS - 12

ER -