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Phosphoglucomutase kinetics with the phosphates of fructose, glucose, mannose, ribose, and galactose.

作者信息

Lowry O H, Passonneau J V

出版信息

J Biol Chem. 1969 Feb 10;244(3):910-6.

PMID:5769188
Abstract
摘要

相似文献

1
Phosphoglucomutase kinetics with the phosphates of fructose, glucose, mannose, ribose, and galactose.磷酸葡萄糖变位酶与果糖、葡萄糖、甘露糖、核糖和半乳糖磷酸盐的动力学。
J Biol Chem. 1969 Feb 10;244(3):910-6.
2
A kinetic study of the effect of alpha-D-galactose, alpha-D-mannose, alpha-D-glucosamine, N-acetyl-alpha-D-glucosamine, and alpha-D-ribose diphosphate on the activity of phosphoglucomutase.α-D-半乳糖、α-D-甘露糖、α-D-氨基葡萄糖、N-乙酰-α-D-氨基葡萄糖和α-D-核糖二磷酸对磷酸葡萄糖变位酶活性影响的动力学研究
J Biol Chem. 1970 Aug 25;245(16):4038-46.
3
Electron paramagnetic resonance studies of manganese (II) coordination in the phosphoglucomutase system.磷酸葡萄糖变位酶系统中锰(II)配位的电子顺磁共振研究。
Biochemistry. 1971 Aug 17;10(17):3190-7. doi: 10.1021/bi00793a005.
4
Synthesis of alpha-D-glucose 1,6-diphosphate, alpha-D-mannose 1,6-diphosphate, alpha-D-ribose 1,5 diphosphate, and N-acetyl-alpha-D-glucosamine 1,6-diphosphate.α-D-葡萄糖1,6-二磷酸、α-D-甘露糖1,6-二磷酸、α-D-核糖1,5-二磷酸和N-乙酰-α-D-葡萄糖胺1,6-二磷酸的合成。
J Biol Chem. 1970 Aug 25;245(16):4031-7.
5
Behavior of cycloaldolase from Neurospora crassa towards substrate analogs and aldolase inhibitors.粗糙脉孢菌中环醇醛缩酶对底物类似物和醛缩酶抑制剂的反应
Biochim Biophys Acta. 1972 Dec 7;289(2):420-7. doi: 10.1016/0005-2744(72)90095-2.
6
Inhibition of phosphoglucomutase by galactose 1-6-diphosphate.1,6-二磷酸半乳糖对磷酸葡萄糖变位酶的抑制作用。
Experientia. 1969 Sep 15;25(9):917-8. doi: 10.1007/BF01898061.
7
The influence of inorganic phosphate and phosphorylated hexoses on the activity of pyruvate kinase.
Arch Biochem Biophys. 1970 Nov;141(1):98-101. doi: 10.1016/0003-9861(70)90111-6.
8
The synthesis of mannose 1-phosphate in brain.脑中磷酸甘露糖-1的合成。
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Transport of sugars into human red blood cell ghosts.糖进入人红细胞血影的转运。
J Cell Physiol. 1966 Jun;67(3):501-6. doi: 10.1002/jcp.1040670314.
10
Synthesis of 4-keto-sugar phosphates.4-酮糖磷酸酯的合成。
Biochem Biophys Res Commun. 1964 Feb 18;15(1):65-9. doi: 10.1016/0006-291x(64)90104-4.

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