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Vanadium ion inhibition of alkaline phosphatase-catalyzed phosphate ester hydrolysis.

作者信息

Lopez V, Stevens T, Lindquist R N

出版信息

Arch Biochem Biophys. 1976 Jul;175(1):31-8. doi: 10.1016/0003-9861(76)90482-3.

DOI:10.1016/0003-9861(76)90482-3
PMID:182081
Abstract
摘要

相似文献

1
Vanadium ion inhibition of alkaline phosphatase-catalyzed phosphate ester hydrolysis.钒离子对碱性磷酸酶催化的磷酸酯水解的抑制作用。
Arch Biochem Biophys. 1976 Jul;175(1):31-8. doi: 10.1016/0003-9861(76)90482-3.
2
[Inhibition of alkaline phosphatase I of Pichia guilliermondii yeast in vitro and in vivo].[季也蒙毕赤酵母碱性磷酸酶I在体内外的抑制作用]
Ukr Biokhim Zh (1978). 1978 Mar-Apr;50(2):212-7.
3
[The kinetics of simultaneous hydrolysis of sodium phenyl phosphate and glycol phosphate catalyzed by alkaline phosphatase].[碱性磷酸酶催化苯基磷酸钠和磷酸甘油酯同时水解的动力学]
Biokhimiia. 1966 May-Jun;31(3):463-7.
4
[The effect of various anions and concentration of buffer solution on the hydrolysis kinetics of sodium phenylphosphate under the action of alkaline phosphatase].[不同阴离子及缓冲溶液浓度对碱性磷酸酶作用下苯磷酸钠水解动力学的影响]
Biokhimiia. 1969 Mar-Apr;34(2):273-6.
5
[Some properties of the alkaline phosphatase of Candida albicans].[白色念珠菌碱性磷酸酶的一些特性]
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6
The free energy of hydrolysis of the phosphoryl-enzyme intermediate in alkaline phosphatase catalyzed reactions.
Biochemistry. 1969 Jun;8(6):2374-80. doi: 10.1021/bi00834a018.
7
Phosphoramidic acids. A new class of nonspecific substrates for alkaline phosphatase from Escherichia coli.磷酰胺酸。一类新型的大肠杆菌碱性磷酸酶非特异性底物。
Biochemistry. 1972 Apr 25;11(9):1616-23. doi: 10.1021/bi00759a012.
8
Hydrolysis of a phosphonate ester catalyzed by an enzyme from Dictyostelium discoideum.
Arch Biochem Biophys. 1979 Oct 1;197(1):364-6. doi: 10.1016/0003-9861(79)90257-1.
9
The kinetics of the Escherichia coli alkaline phosphatase catalyzed hydrolysis of 2,4-dinitrophenyl phosphate.大肠杆菌碱性磷酸酶催化水解2,4-二硝基苯磷酸酯的动力学
J Am Chem Soc. 1967 Dec 20;89(26):7139-40. doi: 10.1021/ja01002a068.
10
Inhibition of human alkaline phosphatases by vanadate.钒酸盐对人碱性磷酸酶的抑制作用。
Biochem J. 1979 Jul 1;181(1):247-50. doi: 10.1042/bj1810247.

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