title: Specific antibodies to bovine choline acetyltransferase raised in mice immunised with small amounts of partially purified enzyme.
abstract: Choline acetyltransferase was purified approximately 18,000-fold from 300 g of bovine caudate nuclei to a specific activity of 21 ?mol min mg protein. The overall procedure used was: extraction of the enzyme by high salt concentration, chromatography on carboxy-methyl-Sephadex, precipitation by ammonium sulphate, affinity chromatography on Blue-Sepharose and, finally absorption on hydroxylapatite. When the enzyme absorbed on hydroxylapatite was injected into mice, it provoked reproducibly a transient production of 'inhibitory' antibodies, followed by higher antibody titres mainly of 'non-inhibitory' type. These responses were elicited by injecting less than a total of 20 ?g of immunogen. The highest antibody titre was obtained less than 2 months following the initial immunisation. Species cross reactivity was investigated. This procedure should prove to be of value in the production of monoclonal antibodies to choline acetyltransferase.
authors.affiliation: Departments of Pharmacology and Human Anatomy, South Parks Road, Oxford, U.K.
authors.forename: L
authors.initials: L
authors.lastname: Eder-Colli
authors.forename: J F
authors.initials: JF
authors.lastname: Powell
authors.forename: A
authors.initials: A
authors.lastname: Claudio Cuello
authors.forename: A
authors.initials: A
authors.lastname: David Smith