Abstract
Summary L-Histidine decarboxylase was stabilized with 1% polyethylene glycol and purified to a homogeneous state from the whole bodies of fetal rats. Antibody was raised in a rabbit against the purified enzyme. The antibody strongly inhibited histidine decarboxylase activity from rat brain as well as that from whole fetal rats, but on Ouchterlony's double difusion it gave a single precipitin line against the fetal enzyme that fused with the line against the brain enzyme with spur formation.
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