IN an earlier investigation1, the molecular weight of α-amylase from pig‘s pancreas2,3 Was found to be 45,000, as calculated from the values4 s20 = 4·50 S, D = 8·05 × 10-7 C.G.S. and V20 = 0·70. At this Institute a new method for the isolation of amylase from malt has been developed5. It was shown that by repeated purification of the albumin fraction from maSlt a preparation was obtained with high α-amylase and β-amylase activity. Therefore it was assumed that the amylase activity of malt is localized in the albumin fraction. By ultracentrifugation of the albumin fraction, only one peak was obtained. It must be stated here that malt-amylase is more polydisperse than α-amylase from pancreas.