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  • 1
    ISSN: 1432-0584
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Zusammenfassung Lösliche Proteine einer Granulafraktion aus menschlichen Neutrophilen wurden einer Acrylamidgel-Elektrophorese (15% Acrylamidgel bei pH 4,3) unterwerfen. Verschiedene Proteinbanden zeigten eine hydrolytische Aktivität gegenü ber Naphthol-AS-D-Chloracetat bei pH 7,4. Die elektrophoretische Wanderung der Naphthol-AS-D-Chloracetat spaltenden Esterase ist ähnlich der von Trypsin, Chymotrypsin und Elastase.
    Notes: Summary Soluble proteins of a granule fraction derived from human neutrophils were subjected to electrophoresis on 15% acrylamide gels at pH 4.3 Several of the protein bands were shown to possess hydrolytic activity on naphthol AS-D chloroacetate at pH 7.4. Electrophoretic movement of NASDCA esterases is similar to those of trypsin, chymotrypsin and elastase.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-1440
    Keywords: Glycogen ; leukocytes ; amyloglucosidase ; Glykogen ; Leukocyten ; Amyloglukosidase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Zusammenfassung An peripheren Blutausstrichen sowie an Kontrollschnitten von Leber, Muskulatur und Schilddrüse wurde die glykogenolytische Wirkung von Amyloglukosidase geprüft. Die Spezifität dieses Enzyms beweist, daß die in den neutrophilen Granulocyten, Thrombocyten und Lymphocyten nachgewiesenen PAS-positiven Substanzen Glykogen darstellen. Die Fixierung in Formalindampf erwies sich für den anschließenden enzymatischen Glykogenabbau als ungeeignet, da nach der Fixierung in Formalindampf im Gegensatz zur Fixierung mit Äthanol, Methanol und Aceton nur ein unvollständiger Glykogenabbau zu erzielen war.
    Notes: Summary Glycogen hydrolytic activity of amyloglucosidase was studied in blood smcars and sections of liver, muscle and thyroid gland. The specificity of amyloglucosidase proved the PAS-positive substances in neutrophil granulocytes, platelets and lymphocytes to be glycogen. Fixation of the material with formalin was unsuitable as the glycogenolytic activity of amyloglucosidase was reduced after this fixation. This was possibly due to inadequate penetration of the enzyme into the cell after formalin fixation.
    Type of Medium: Electronic Resource
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