Abstract— We have examined the subcellular localization of histamine, histamine methyltransferase (EC 184.108.40.206) (HMT) and histidine decarboxylase (EC 220.127.116.11) in rat hypothalamus after osmotic lysis of synaptosome‐containing primary particulate fractions. When crude mitochondrial fractions are subjected to osmotic lysis, histamine is retained within particulate structures, while HMT is released into the supernatant fluid. The majority of histidine decarboxylase activity is also recovered in the supernatant fluid, although more histidine decarboxylase than HMT is retained in particulate fractions. After sucrose gradient fractionation of osmotically lysed crude mitochondrial or microsomal pellets, histamine is also retained in particulate structures, with the greatest amount occurring in a fraction enriched in synaptic vesicles. In these sucrose gradients histidine decarboxylase activity shows a greater particulate localization than does HMT activity.
|Original language||English (US)|
|Number of pages||9|
|Journal||Journal of Neurochemistry|
|State||Published - Jul 1974|
ASJC Scopus subject areas
- Cellular and Molecular Neuroscience