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Immunohistochemical analysis of the cross-reaction of anti-rat histidine decarboxylase antibody with guinea-pig DOPA decarboxylase.

Authors
  • Taguchi, Y
  • Watanabe, T
  • Shiosaka, S
  • Tohyama, M
  • Wada, H
Type
Published Article
Journal
Brain Research
Publisher
Elsevier
Publication Date
Aug 12, 1985
Volume
340
Issue
2
Pages
235–242
Identifiers
PMID: 3896404
Source
Medline
Language
English
License
Unknown

Abstract

L-Histidine decarboxylase [L-histidine carboxylyase, HDC, EC 4.1.1.22] is an enzyme distinct from L-DOPA decarboxylase [L-aromatic amino acid carboxylyase, DDC, EC 4.1.1.28]: the two decarboxylases from fetal rat liver were completely separated from each other by DEAE-cellulose column chromatography and by affinity chromatography with L-carnosine as a ligand. The antibody raised against this HDC inhibited the HDC's from rat and guinea-pig brains very strongly, but their DDCs very weakly. However, in immunofluorescent histochemical studies, the antibody cross-reacted with DDC-like immunoreactive structures, such as chromaffin cells of the adrenal medulla, the raphe nucleus, the substantia nigra, and the locus coeruleus of the brain of guinea-pigs, but not of rats, suggesting that these two decarboxylases share some antigenic structures.

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