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- W2041103656 abstract "Two histadine decarboxylase activities have been found in rat stomach. One, in the supernatant fraction of stomach homogenate, had optimum activity at pH 7 and appeared similar to the specific mammalian L-histidine decarboxylase (EC 4.1.1.22) descrideb by other workers. The second, in the insoluble residue of stomach homogenate, had a pH optimum of 5 and resembled the Lactobacillus L-histidine decarboxylase (EC 4.1.1.22). This second, residue enzyme was located in the upper part of normal rat stomach, an area which supported a heavy growth of Lactobacillus. The residue histidine decarboxylase activity was absent in germ-free rat stomach and was therefore thought to be of bacterial origin. In view of the coprophagic activity of rats, feces could serve as an inoculum of Lactobacillus in stomach, and the levels of activity of the residue enzyme were found to be related to the state of cleanliness of the animal cages. Other factors, such as starvation and drug treatment, which affect the levels of the residue enzyme are discussed. There was also evidence that the histamine content of stomach is related in part to the activity of the residue histidine decarboxylase." @default.
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- W2041103656 date "1970-07-01" @default.
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- W2041103656 title "Bacterial histidine decarboxylase in rat stomach" @default.
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- W2041103656 doi "https://doi.org/10.1016/0014-2999(70)90052-x" @default.
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