Immunoaffinity Purification of Human Choline Acetyltransferase: Comparison of the Brain and Placental Enzymes

Gordon Bruce, Bruce H. Wainer, Louis B. Hersh

Research output: Contribution to journalArticle

192 Citations (Scopus)

Abstract

Abstract: A rapid and efficient immunoaffinity purification procedure has been developed for human placental choline acetyltransferase (ChAT). Using this procedure, human placental ChAT was purified to homogeneity with high recovery of enzyme activity (50–60%). Purified ChAT was used to raise a monospecific anti‐human ChAT polyclonal antibody in rabbits. A comparison of the physical properties of ChAT was made between the enzymes purified from human brain and human placenta. Only one form of the enzyme exists in either tissue, having identical molecular weights of 68,000 and a single apparent pI of 8.1. A more detailed comparison of the two enzymes using peptide mapping and epitope mapping indicates identity between the brain and placental enzymes.

Original languageEnglish (US)
Pages (from-to)611-620
Number of pages10
JournalJournal of Neurochemistry
Volume45
Issue number2
DOIs
StatePublished - 1985

Fingerprint

Choline O-Acetyltransferase
Purification
Brain
Enzymes
Epitope Mapping
Peptide Mapping
Enzyme activity
Placenta
Epitopes
Physical properties
Molecular Weight
Molecular weight
Tissue
Rabbits
Recovery
Peptides
Antibodies

Keywords

  • Choline acetyltransferase
  • Immunoaffinity purification
  • Polyclonal choline acetyltransferase antibody

ASJC Scopus subject areas

  • Biochemistry
  • Cellular and Molecular Neuroscience

Cite this

Immunoaffinity Purification of Human Choline Acetyltransferase : Comparison of the Brain and Placental Enzymes. / Bruce, Gordon; Wainer, Bruce H.; Hersh, Louis B.

In: Journal of Neurochemistry, Vol. 45, No. 2, 1985, p. 611-620.

Research output: Contribution to journalArticle

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