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PROPERTIES AND REGIONAL DISTRIBUTION OF HISTIDINE DECARBOXYLASE IN RAT BRAIN
Author(s) -
Schwartz J. C.,
Lampart C.,
Rose C.
Publication year - 1970
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1970.tb03722.x
Subject(s) - histidine decarboxylase , histidine , histamine , enzyme , substrate (aquarium) , chemistry , biochemistry , benzene , aromatic l amino acid decarboxylase , stereochemistry , biology , endocrinology , organic chemistry , ecology
—Properties of the histamine‐forming enzyme in rat brain were studied, utilizing a sensitive fluorometric assay. The optimum pH was related to substrate concentration and found to be6·4 at 10 −2 m ‐histidine; the apparent K m was about 4·10 −4 m ; enzyme activity was inhibited by α‐hydrazino ‐histidine and brocresine but was not affected by α‐methyl DOPA or benzene. These different data suggest that the 'specific’histidine decarboxylase (EC 4.1.1.22)—and not the aromatic l ‐aminoacid decarboxylase—is involved. Determination of enzyme activity and histamine level in different areas of the rat brain revealed important regional differences, the two values being roughly parallel.