Abstract
Abstract Histidine decarboxylase activity has been demonstrated in some experimental tumours by direct enzyme assay. The kinetic properties of semi-purified preparations of the histamine-forming enzyme from Rous rat sarcoma and Walker rat mammary carcinoma were similar to those of the “specific” histidine decarboxylase of the foetal rat. Transplants from a malignant hamster melanoma had no “specific” histidine decarboxylase but high dopa decarboxylase activity. The lack of histidine decarboxylase in this tumour seems to indicate that a high histamine-forming capacity is not indispensable for tumour growth.
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