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 Scopus citations

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 - Aug 1985

Keywords

  • Choline acetyltransferase
  • Immunoaffinity purification
  • Polyclonal choline acetyltransferase antibody

ASJC Scopus subject areas

  • Biochemistry
  • Cellular and Molecular Neuroscience

Fingerprint Dive into the research topics of 'Immunoaffinity Purification of Human Choline Acetyltransferase: Comparison of the Brain and Placental Enzymes'. Together they form a unique fingerprint.

  • Cite this