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果蝇Kc细胞中β-N-乙酰-D-氨基葡萄糖苷酶和β-N-乙酰-D-己糖胺酶的物理性质

Physical properties of beta-N-acetyl-D-glucosaminidase and beta-N-acetyl-D-hexosaminidase from Drosophila Kc-cells.

作者信息

Sommer U, Spindler K D

机构信息

Institut für Zoologie, Heinrich-Heine-Universität Düsseldorf, Federal Republic of Germany.

出版信息

Arch Insect Biochem Physiol. 1991;18(1):45-53. doi: 10.1002/arch.940180105.

Abstract

Kc-cells from Drosophila produce two different beta-D-hexosaminidases, a beta-N-acetyl-D-glucosaminidase (E.C.3.2.1.30) and a beta-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 degrees C) for both enzymes if p-nitrophenyl-N-acetylglucosaminide is used as a substrate. However, when p-nitrophenyl-N-acetylgalactosaminide is used as the substrate the beta-N-acetyl-D-hexosaminidase has a temperature optimum about 10 degrees C higher. With higher salt concentrations, the activity of the beta-N-acetyl-D-glucosaminidase increases, whereas beta-N-acetyl-D-hexosaminidase is inhibited. Both enzymes also differ in their sensitivity to urea, the beta-N-acetyl-D-hexosaminidase being less sensitive than the beta-N-acetyl-D-glucosaminidase.

摘要

果蝇的Kc细胞产生两种不同的β-D-己糖胺酶,一种是β-N-乙酰-D-葡糖胺酶(E.C.3.2.1.30),另一种是β-N-乙酰-D-己糖胺酶(E.C.3.2.1.52),它们也分泌到培养基中。两种酶的相对分子质量约为126,000±9,700;沉降系数为8.37±0.44。两种酶在pH 5.5时具有大致相同的最适pH值和相同的热稳定性。如果使用对硝基苯基-N-乙酰葡糖胺作为底物,两种酶的最适温度相同(50℃)。然而,当使用对硝基苯基-N-乙酰半乳糖胺作为底物时,β-N-乙酰-D-己糖胺酶的最适温度约高10℃。在较高盐浓度下,β-N-乙酰-D-葡糖胺酶的活性增加,而β-N-乙酰-D-己糖胺酶受到抑制。两种酶对尿素的敏感性也不同,β-N-乙酰-D-己糖胺酶比对β-N-乙酰-D-葡糖胺酶的敏感性低。

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