胰岛中葡萄糖激酶的色谱分辨率及动力学特性
Chromatographic resolution and kinetic characterization of glucokinase from islets of Langerhans.
作者信息
Meglasson M D, Burch P T, Berner D K, Najafi H, Vogin A P, Matschinsky F M
出版信息
Proc Natl Acad Sci U S A. 1983 Jan;80(1):85-9. doi: 10.1073/pnas.80.1.85.
Abstract
Glucokinase (ATP:D-glucose 6-phosphotransferase, EC 2.7.1.2) from rat islets of Langerhans was partially purified by chromatography on DEAE-Cibacron blue F3GA agarose. The enzyme eluted in two separate peaks. Sigmoidal rate dependence was found with respect to glucose (Hill coefficient = 1.5) for both enzyme fractions. Km values for glucose were 5.7 mM for the major fraction and 4.5 mM for the minor fraction. Neither fraction phosphorylated GlcNAc. A GlcNAc kinase (ATP:2-acetamido-2-deoxy-D-glucose 6-phosphotransferase, EC 2.7.1.59)-enriched fraction, prepared by affinity chromatography on Sepharose-N-(6-aminohexanoyl)-GlcNAc, had a Km of 25 microM for GlcNAc. Islet tissue also contained hexokinase (ATP:D-hexose 6-phosphotransferase, EC 2.7.1.1) eluting in multiple peaks. The results are consistent with the concept that glucokinase serves as the glucose sensor of pancreatic beta cells.
摘要
通过在DEAE-汽巴蓝F3GA琼脂糖上进行层析，对来自大鼠胰岛的葡萄糖激酶（ATP：D-葡萄糖6-磷酸转移酶，EC 2.7.1.2）进行了部分纯化。该酶以两个独立的峰洗脱。两种酶组分对葡萄糖均呈现S形速率依赖性（希尔系数 = 1.5）。主要组分的葡萄糖Km值为5.7 mM，次要组分的葡萄糖Km值为4.5 mM。两种组分均不使N-乙酰葡糖胺磷酸化。通过在琼脂糖-N-(6-氨基己酰基)-N-乙酰葡糖胺上进行亲和层析制备的富含N-乙酰葡糖胺激酶（ATP：2-乙酰氨基-2-脱氧-D-葡萄糖6-磷酸转移酶，EC 2.7.1.59）的组分，其对N-乙酰葡糖胺的Km值为25 μM。胰岛组织中还含有以多个峰洗脱的己糖激酶（ATP：D-己糖6-磷酸转移酶，EC 2.7.1.1）。这些结果与葡萄糖激酶作为胰腺β细胞葡萄糖传感器的概念一致。
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