RAT ADRENAL DOPAMINE‐β‐HYDROXYLASE PURIFICATION AND IMMUNOLOGIC CHARACTERISTICS
- 1 November 1976
- journal article
- research article
- Published by Wiley in Journal of Neurochemistry
- Vol. 27 (5), 1091-1096
- https://doi.org/10.1111/j.1471-4159.1976.tb00313.x
Abstract
Dopamine-β-hydroxylase (DBH) was purified from rat adrenal medulla by a series of steps including sedimentation of membranes, extraction with n-butanol, ammonium sulfate fractionation, gel chromatography and ion-exchange chromatography. Disk gel electrophoresis revealed two protein bands, both of which were active. Antiserum was prepared against homogeneously purified bovine adrenal and rat adrenal DBH: Ouchterlony immunodiffusion, enzyme neutralization and complement fixation tests demonstrated that the respective homologous antisera were monospecific and of high titer. Antiserum to bovine DBH was only 2- to 3-fold more potent than pre-immune serum in inhibition of rat DBH activity. Complement fixation tests demonstrate that antiserum to bovine DBH has a 25,000-fold lower immunoreactivity with rat DBH than with bovine DBH.Keywords
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