Chromatographic resolution and kinetic characterization of glucokinase from islets of Langerhans.
Chromatographic resolution and kinetic characterization of glucokinase from islets of Langerhans.
复制标题
朗格汉斯岛葡萄糖激酶的色谱分离度和动力学表征。
DOI:
10.1073/pnas.80.1.85
复制
发表时间:
1983
影响因子:
11.1
通讯作者:
Matschinsky,FM
中科院分区:
文献类型:
--
作者:
Meglasson,MD;Burch,PT;Berner,DK;Najafi,H;Vogin,AP;Matschinsky,FM
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.
DOI:
--
发表时间:
1980
期刊:
Biochimica et Biophysica Acta
影响因子:
--
作者:
M. B. Allen;J. L. Brockelbank;D. G. Walker
通讯作者:
D. G. Walker