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Demonstration of β-N-acetyl-D-glucosaminidase and β-N-acetyl-D-hexosaminidase in Drosophila Kc-cells

✍ Scribed by Ulrich Sommer; Prof. Dr. Klaus-Dieter Spindler

Publisher
John Wiley and Sons
Year
1991
Tongue
English
Weight
589 KB
Volume
17
Category
Article
ISSN
0739-4462

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✦ Synopsis

K,-cells from Drosophila melanogaster, grown under serum-free conditions, produce two p-hexosaminidases and secrete these enzymes into the medium. The two enzymes were separated by DEAE-exchange chromatography. According to their substrate specificities one enzyme is a f3-N-acetyl-D-glucosarninidase (E.C.3.2.1.30), the other one a P-N-acetyl-D-hexosaminidase (E.C.3.2.1.52). The P-N-acetyl-D-glucosaminidase is predominant in the medium, the 6-Nacetyl-D-hexosaminidase within the cells. The K , values for the substrates pNP-GlcNAc, pNP-CalNAc, and (GICNAC)~ are 0.8,16.73, and 1.67 m M for the p-N-acetyl-D-glucosaminidase and 0.24,0.44, and 0.2 rnM for the P-N-acetyl-D-hexosaminidase. Both enzymes are inhibited by the products and the P-N-acetyl-D-glucosarninidase is also inhibited stereospecifically by the substrates pNP-GlcNAc and (GICNAC)~. Both enzymes are inhibited in a partial competitive way by acetamidolactones, the Kis being as low as 0.1 pM.

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