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Purified isoenzymes of human alkaline phosphatase from placenta, intestine and liver were investigated as catalysts for phosphotransferase activity, using the phosphoacceptors Tris, 2-amino-2-methyl-1-propanol, 2-amino-2-methyl-1,3-propanediol, diethanolamine, 2-(ethylamino)ethanol, ethanolamine, and N-methyl-D-glucamine. All of the compounds supported(More)
Normal erythrocytes were subject to swelling and some haemolysis when suspended in a NaCl-formaldehyde-Na(2)EDTA diluent of pH 4.9 for routine blood-cell counting in the Coulter counter. A phosphate-buffered saline of pH 7.4 was substituted and has proven satisfactory for total erythrocyte counts. Polyvinyltoluene latex was unsuitable for volume calibration(More)
Ghosts of human erythrocytes prepared by hypotonic hemolysis were assayed for aldolase, triosephosphate isomerase, glyceraldehyde phosphate dehydrogenase, phosphoglycerate kinase, pyruvate kinase, lactate dehydrogenase, and glutathione peroxidase and reductase. Cryptic activity of the enzymes was demonstrated by an increase in activity on dilution with(More)