Summary
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.
Zusammenfassung
Lösliche Proteine einer Granulafraktion menschlicher Granulozyten wurden bei pH 4.3 mittels Acrylamid-Gelelektrophorese aufgetrennt. Die Gele wurden anschließend auf Peroxydaseaktivität und Aktivitäten von 11 Hydrolasen untersucht. Die Hydrolasen waren: saure Phosphatase, alkalische Phosphatase, Alaninaminopeptidase, Arylsulfatase, β-Galaktosidase, β-Glucuronidase, Leucinaminopeptidase, α-Naphthylacetatesterase Naphthol-AS-D-acetatesterase, Naphthol-AS-D-chloracetatesterase und Lysozym. Die Proteine mit der größten zur Kathode gerichteten Wanderungsgeschwindigkeit zeigten ausschließlich Esteraseaktivität (12 Banden) gegenüber den 3 getesteten Ester-Substraten und Lysozymaktivität (1 Bande). 2 der Esterasebanden waren stark basisch und wanderten schneller als das Lysozym. Die Esteraseaktivität konnte mit Diisopropylfluorphosphat gehemmt werden.
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Rindler, R., Braunsteiner, H. Soluble proteins from human leukocyte granules. Blut 27, 26–32 (1973). https://doi.org/10.1007/BF01631423
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DOI: https://doi.org/10.1007/BF01631423