Abstract
The original methods for measuring d-amino acid oxidase in animal tissues involved the use of either phosphate buffer (Krebs, 1935), phosphate buffer with added arsenite (Rodney and Garner, 1938), both at about pH 7.5, or pyrophosphate buffer at pH 8.6 (Krebs, 1939). The two papers found which contain values for this enzyme in chicken tissue (Trufanov and Pavlova, 1951; Williams et at., 1949) described methods employing phosphate buffer. A study of the effect of buffer and pH on the assay of purified pig kidney d-amino acid oxidase by Walaas and Walaas (1949) revealed that pyrophosphate buffer at pH 8.3 gave optimum results. Pyrophosphate buffer appears to have been used more frequently than phosphate buffer in mammalian studies (Burton, 1955). This note presents the results of comparisons of these and other buffer systems used in the measurement of this enzyme in chicken tissue.The buffer systems were compared in the following …
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