For the study of alkaline phosphatase systems a non-phosphate-containing buffer is required. The buffers in common use for the alkaline pH range are ammonia, borate, glytine and veronal. Ammonia and borate have a retarding effect on the rate of ,enzymic hydrolysis of phosphoric esters. Glycine activates phosphatase when present in very low concentrations (0 1-1 mm), but in the concentrations used in the buffer system (0-01-01M) it has an undoubted inhibitory effect. Veronal is much better in this respect, but its useful pH range (6-8-9-6) is not sufficiently high to cover the pH optima of the enzyme acting on aromatic phosphoric esters (Delory & King, 1943). To satisfy the criteria of non-inhibition of enzymic action, useful alkaline pH range, simplicity and reasonable stability, a mixture of sodium carbonate with bicarbonate has been investigated. The range covered, 9-2-10

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