Abstract
Histidine decarboxylase activity was found in the kidneys of newborn infants dying in the first week of life. Smaller amounts were found in liver, lung, stomach, spleen, bone marrow and skin. The enzyme had the char-acteristics of nonspecific histidine decarboxylase, being active at pH 8-9 and potentiated by benzene. There was no significant difference in enzyme activity between infants dying of hyaline membrane disease and infants dying from other causes. This does not support the hypothesis that the beneficial effects of antihistamine drugs in respiratory distress are due to specific antagonism of histamine present in excess. There was evidence of slight histidine decarboxylating activity at pH 6.5 in skin, but not in other tissues. However, the presence of relatively large amounts of preformed histamine made its significance difficult to assess. Removal of the preformed histamine by dialysis did not help to identify the enzyme more accurately, because dialysis reduced the decarboxylating activity present.

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