The deaminases of adenosine and adenylic acid in blood and tissues

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Abstract
The effects of time, substrate conc., dilution, pH, specific buffer and tissue inhibitions etc. were studied for the adenosine and adenylic acid deaminases as they appeared in blood and tissue extracts. Adenosine deaminase was independent of substrate conc. beyond a very small level (ca. 0.005%), being independent of the dilution and the type of buffer used. Adenylic acid deaminase acted proportionally to the substrate conc. up to a very high figure (over 1%) which arose from the action of specific tissue and blood inhibitors. This deaminase was also specifically inhibited by certain buffers (veronal, phosphoric acid, etc.) but not appreciably by citric or maleic acids. Its effect was considerably increased by dilution. Voluntary muscle contained 40 times more adenylic acid deaminase than any other tissue in the rabbit, but its effective action was about 500-1000 times or more greater, owing to the absence or ineffective action therein of the specific tissue inhibitors. Methods for determining the path of the deamination of adenine nucleotide were given. Nerve tissue, the auricle of the heart and red corpuscles deaminated adenylic acid normally in a direct way, but the general visceral deamination was indirect and took place after an initial dephos-phorylation. The distr. of adenosine and adenylic acid deaminases was studied for 36 tissues of the rabbit. The highest conc. of adenosine deaminase was found in the vermiform appendix and somewhat lesser amts. in duodenum and jejunum. Contrary to Lohmann"s finding adenylic acid deaminase was found in very appreciable amts. in the claw muscles of the crab.

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