Abstract
Soluble granule proteins from human granulocytes were subjected to acrylamide-gel electrophoresis at pH 4.3. The gels subsequently were reacted for peroxidase and 11 hydrolytic enzymes (i.e. acid phosphatase, alkaline phosphatase, alanine aminopeptidase, arylsulphatase, β-galactosidase, β-glucuronidase, leucine aminopeptidase, α-naphthylacetate esterase, naphthol AS-D acetate esterase, naphthol AS-D chloroacetate esterase and lysozyme). Out of these activities only esterase activity (12 bands) on the 3 ester substrates and lysozyme activity (1 band) could be identified with the proteins showing high cathodal migration. 2 of the proteins showing esterase activity migrated faster to the cathode than the lysozyme. Esterase activity was sensitive to di-isopropylfluorophosphate.
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