Histidine Decarboxylase: Isolation and Molecular Characteristics

Overview

Journal Neurochem Res

Specialties Chemistry
Neurology

Date 1984 Jul 1

PMID 6504233

Citations 4

Authors

R Grzanna

Affiliations

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Abstract

High levels of histidine decarboxylase activity were measured in rat basophilic leukemia cells grown in ascitic form in 4 week old WKY/N rats. The potent inhibition of this enzyme by brocresine and alpha-methylhistidine but not by alpha-methyl DOPA identified it as a specific histidine decarboxylase. Gel filtration and polyacrylamide gel electrophoresis revealed a molecular weight of 125,000 for the native enzyme, similar to that of fetal rat liver histidine decarboxylase. Using rat basophilic leukemia cells as starting material, histidine decarboxylase was purified extensively in a seven step procedure. Electrophoresis under denaturing conditions revealed that histidine decarboxylase is a dimeric protein consisting of two identical subunits with a molecular weight of 62,000. The results indicate that rat basophilic leukemia cells provide a new and rich source for the purification of histidine decarboxylase.

Citing Articles

Mapping of catalytically important residues in the rat L-histidine decarboxylase enzyme using bioinformatic and site-directed mutagenesis approaches.

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PMID: 14961766 PMC: 1224094. DOI: 10.1042/BJ20031525.

The regulation of histidine decarboxylase gene expression.

Hocker M, Zhang Z, Koh T, Wang T Yale J Biol Med. 1997; 69(1):21-33.

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Alpha-fluoromethylhistidine in the treatment of idiopathic cold urticaria.

Neittaanmaki H, Fraki J, Harvima R, Forstrom L Arch Dermatol Res. 1989; 281(2):99-104.

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Histidine decarboxylase from rat and rabbit brain: partial purification and characterization.

Chudomelka P, RAMALEY R, Murrin L Neurochem Res. 1990; 15(1):17-24.

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