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A procedure for the purification of neutral maltase from human polymorphonuclear leukocytes is described, involving solubilization with Triton X-100, proteolytic attack and three chromatographic steps: DEAE ion exchange, AcA 22 gel filtration and a second DEAE chromatography. The enzyme was obtained with a final specific activity of 30 units/mg of protein, comparable with that of other neutral maltases previously purified. The Mr of the enzyme was 550000 as determined by gel filtration. SDS/polyacrylamide-gel electrophoresis, under non-denaturing conditions, led to a major band of 500000 and a minor one of 260000, both active, suggesting a polymeric or aggregated form of the protein. The catalytic properties of the human granulocytic neutral maltase were investigated. The pH optimum was around 6. The enzyme exhibited a broad range of substrate specificity, hydrolysing di-and oligosaccharides with a(l -+ 2), a(l -+ 3) and z(1 -. 4) glucosidic linkages. The highest activities were observed for a(l -.4) glucose oligomers of three to five residues. It was also found to hydrolyse polysaccharides such as starch and glycogen. The results of the inhibition studies are interpreted in terms of the existence of a large site including several subsites. The enzyme properties are broadly similar to those observed for other purified neutral a-glucosidases, in particular that of human kidney origin. INTRODUCTIONNeutral maltases (a.-D-glucoside glucohydrolases, EC 3.2.1.20) are a-glucosidases which split glucose residues from the non-reducing ends of various a-glycans ranging