兔骨骼肌糖原磷酸化酶的31P核磁共振研究：磷酸吡哆醛的电离状态
31P nuclear magnetic resonance studies of glycogen phosphorylase from rabbit skeletal muscle: ionization states of pyridoxal 5'-phosphate.
作者信息
Feldmann K, Hull W E
出版信息
Proc Natl Acad Sci U S A. 1977 Mar;74(3):856-60. doi: 10.1073/pnas.74.3.856.
Abstract
31P nuclear magnetic resonance (NMR) at 72.8 MHZ has been used to study glycogen phosphorylase from rabbit muscle (1,4-alpha-D-glucan:orthophosphate alpha-glucosyltransferase, EC 2.4.1.1) at concentrations as low as 25 mg/ml, using a WH-180 wide-bore superconducting spectrometer. The use of a thio analogue for 5'-AMP and arsenate for inorganic phosphate allowed the observation of three distinct forms of enzyme-bound pyridoxal 5'-phosphate at --0.2 ppm (Form I), --2 to --3 ppm (Form II), and --3.5 ppm (Form III) relative to triethylphosphate. Conversion of I to III occurs by activation of phosphorylase either by formation of a ternary complex of phosphorylase b with effector and arsenate or, more efficiently, by direct phosphorylation to give the a form of the enzyme. The ionization state and exposure to solvent of each of the three forms is inferred from the 31P NMR data.
摘要
使用WH - 180宽口径超导光谱仪，在72.8兆赫兹下的31P核磁共振（NMR）已用于研究浓度低至25毫克/毫升的兔肌肉糖原磷酸化酶（1,4 - α - D - 葡聚糖：正磷酸α - 葡糖基转移酶，EC 2.4.1.1）。使用5'-AMP的硫代类似物和无机磷酸盐的砷酸盐，相对于三乙基磷酸，可观察到酶结合的磷酸吡哆醛的三种不同形式，分别在-0.2 ppm（形式I）、-2至-3 ppm（形式II）和-3.5 ppm（形式III）处。I向III的转化是通过磷酸化酶与效应物和砷酸盐形成三元复合物来激活磷酸化酶，或者更有效地通过直接磷酸化产生酶的a形式来实现。从31P NMR数据推断出三种形式中每种形式的电离状态和对溶剂的暴露情况。
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