ISSN:
0739-4462
Schlagwort(e):
molecular mass
;
pH and temperature optima
;
thermal stability
;
influence of ionic strength
;
Chemistry
;
Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
Quelle:
Wiley InterScience Backfile Collection 1832-2000
Thema:
Biologie
Notizen:
Kc-cells from Drosophila produce two different β-D-hexosaminidases, a β-N-acetyl-D-glucosaminidase (E.C.3.2.1.30) and a β-N-acetyl-D-hexosaminidase (E.C.3.2.1.52), which are also secreted into the medium. The Mr of both enzymes is about 126,000 ± 9,700; the S-values are 8.37 ± 0.44. Both enzymes have about the same pH optima at 5.5 and the same thermal stability. The temperature optima are identical (50°C) for both enzymes if p-nitrophenyl-N-acetylglucosaminide is used as a substrate. However, when p-nitrophenyl-N-acetylgalactoseaminide is used as the substrate the β-N-acetyl-D-hexosaminidase has a temperature optimum about 10°C higher. With higher salt concentrations, the activity of the β-N-acetyl-D-glucosaminidase increases, whereas β-N-acetyl-D-hexosaminidase is inhibited. Both enzymes also differ in their sensitivity to urea, the β-N-acetyl-D-hexosaminidase being less sensitive than the β-N-acetyl-D-glucosaminidase.
Zusätzliches Material:
7 Ill.
Materialart:
Digitale Medien
URL:
http://dx.doi.org/10.1002/arch.940180105
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