C. Dartsch et L. Persson, RECOMBINANT EXPRESSION OF RAT HISTIDINE-DECARBOXYLASE - GENERATION OFANTIBODIES USEFUL FOR WESTERN-BLOT-ANALYSIS, International journal of biochemistry & cell biology, 30(7), 1998, pp. 773-782
Histidine decarboxylase catalyses the formation of histamine, an impor
tant biological messenger. In spite of the essential biological functi
ons exerted by histamine the knowledge about the mechanisms involved i
n the regulation of histidine decarboxylase is rather limited. This is
most likely due to the limited supply of suitable tools, including hi
ghly specific antibodies. In the present study we describe the product
ion and characterisation of specific antisera against rat histidine de
carboxylase using recombinant protein synthesised in a bacterial expre
ssion system. The antisera were shown to effectively immunoprecipitate
histidine decarboxylase activity in extracts of fetal rat liver as we
ll as to detect the histidine decarboxylase protein by Western blot an
alysis of COS-7 cells expressing recombinant rat histidine decarboxyla
se. The results demonstrate the successful production of highly specif
ic antisera to histidine decarboxylase which may become valuable tools
in future studies of the structure and function of this enzyme. (C) 1
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