大鼠肝脏中的内切-N-乙酰-β-D-氨基葡萄糖苷酶活性。底物特异性、酶抑制、亚细胞定位及部分纯化的研究。
Endo-N-acetyl-beta-D-glucosaminidase activity in rat liver. Studies on substrate specificity, enzyme inhibition, subcellular localization and partial purification.
作者信息
Lisman J J, van der Wal C J, Overdijk B
出版信息
Biochem J. 1985 Jul 15;229(2):379-85. doi: 10.1042/bj2290379.
Abstract
Endo-N-acetyl-beta-D-glucosaminidase (EC 3.2.1.96, endoglucosaminidase) has been partially purified (520-fold with respect to the cytoplasmic activity) by using concanavalin A-Sepharose, CM-Sephadex and Bio-Gel P-150 chromatography. From the influence of exogenous glycopeptides on the endoglucosaminidase activity it can be concluded that this activity consists of one enzyme hydrolysing both N-acetyl-lactosaminic-type and oligomannosidic-type substrates. Glycoproteins present in the homogenate inhibit the endoglucosaminidase activity. On re-examination of the subcellular distribution of endoglucosaminidase (after removal of inhibiting glycoproteins from the respective subcellular fractions), its cytoplasmic localization was confirmed.
摘要
内切-N-乙酰-β-D-氨基葡萄糖苷酶（EC 3.2.1.96，内切葡糖胺酶）已通过使用伴刀豆球蛋白A-琼脂糖、CM-葡聚糖凝胶和Bio-Gel P-150色谱法进行了部分纯化（相对于细胞质活性提高了520倍）。从外源性糖肽对内切葡糖胺酶活性的影响可以得出结论，该活性由一种能水解N-乙酰乳糖胺型和寡甘露糖型底物的酶组成。匀浆中存在的糖蛋白会抑制内切葡糖胺酶的活性。在内切葡糖胺酶的亚细胞分布重新检查时（从各个亚细胞组分中去除抑制性糖蛋白后），证实了其在细胞质中的定位。
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