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The reaction of glutamate dehydrogenase with 4-iodoacetamido salicylic acid.

作者信息

Malcolm A D, Radda G K

出版信息

Eur J Biochem. 1970 Sep;15(3):555-61. doi: 10.1111/j.1432-1033.1970.tb01040.x.

DOI:10.1111/j.1432-1033.1970.tb01040.x
PMID:5465997
Abstract
摘要

相似文献

1
The reaction of glutamate dehydrogenase with 4-iodoacetamido salicylic acid.谷氨酸脱氢酶与4-碘乙酰氨基水杨酸的反应。
Eur J Biochem. 1970 Sep;15(3):555-61. doi: 10.1111/j.1432-1033.1970.tb01040.x.
2
Methionyl residue critical for activity and regulation of bovine liver glutamate dehydrogenase.甲硫氨酰残基对牛肝谷氨酸脱氢酶的活性和调节至关重要。
J Biol Chem. 1973 Nov 10;248(21):7359-69.
3
Studies of glutamate dehydrogenase. Identification of an amino group involved in the substrate binding.谷氨酸脱氢酶的研究。参与底物结合的氨基的鉴定。
Eur J Biochem. 1974 Feb 1;41(3):603-6. doi: 10.1111/j.1432-1033.1974.tb03302.x.
4
The effect of modifying lysine-126 on the physical, catalytic and regulatory properties of bovine liver glutamate dehydrogenase.修饰赖氨酸-126对牛肝谷氨酸脱氢酶物理、催化及调节特性的影响
Biochem J. 1973 May;133(1):173-82. doi: 10.1042/bj1330173.
5
Chemical modification of the catalytic, regulatory, and physical properties of glutamate dehydrogenase by trinitrobenzene sulfonate.三硝基苯磺酸对谷氨酸脱氢酶催化、调节及物理性质的化学修饰
Arch Biochem Biophys. 1971 Mar;143(1):158-65. doi: 10.1016/0003-9861(71)90196-2.
6
Regulation of glutamate dehydrogenase by histidine.组氨酸对谷氨酸脱氢酶的调节作用。
Biochim Biophys Acta. 1971 Feb 10;227(2):241-7. doi: 10.1016/0005-2744(71)90057-x.
7
Distance relationships between the catalytic site labeled with 4-(iodoacetamido)salicylic acid and regulatory sites of glutamate dehydrogenase.用4-(碘乙酰胺基)水杨酸标记的催化位点与谷氨酸脱氢酶调节位点之间的距离关系。
Biochemistry. 1984 Aug 14;23(17):3789-99. doi: 10.1021/bi00312a001.
8
Identification of the sites of modification of bovine liver glutamate dehydrogenase reacted with trinitrobenzenesulfonate.与三硝基苯磺酸反应的牛肝谷氨酸脱氢酶修饰位点的鉴定
Biochemistry. 1971 Sep 14;10(19):3516-26. doi: 10.1021/bi00795a005.
9
The site at which 4-iodoacetamidosalicylate reacts with glutamate dehydrogenases.4-碘乙酰氨基水杨酸与谷氨酸脱氢酶反应的位点。
Biochem J. 1973 May;133(1):165-71. doi: 10.1042/bj1330165.
10
Relationship between stability and state of association in glutamate dehydrogenase.谷氨酸脱氢酶中稳定性与缔合状态之间的关系。
Biochim Biophys Acta. 1969 Jul 8;185(1):9-18. doi: 10.1016/0005-2744(69)90277-0.

引用本文的文献

1
Some classical errors in the kinetic analysis of enzyme reactions.酶反应动力学分析中的一些经典错误。
Biochem J. 1993 Nov 1;295 ( Pt 3)(Pt 3):898-9. doi: 10.1042/bj2950898.
2
Experimental approach to the kinetic study of unstable site-directed irreversible inhibitors: kinetic origin of the apparent positive co-operativity arising from inactivation of trypsin by p-amidinophenylmethanesulphonyl fluoride.不稳定的定点不可逆抑制剂动力学研究的实验方法:对氨基苯甲脒基甲磺酰氟使胰蛋白酶失活产生的表观正协同性的动力学起源
Biochem J. 1994 Apr 1;299 ( Pt 1)(Pt 1):29-35. doi: 10.1042/bj2990029.
3
Kinetics of protein modification reactions.
蛋白质修饰反应的动力学
Biochem J. 1984 Jan 15;217(2):341-51. doi: 10.1042/bj2170341.
4
The site at which 4-iodoacetamidosalicylate reacts with glutamate dehydrogenases.4-碘乙酰氨基水杨酸与谷氨酸脱氢酶反应的位点。
Biochem J. 1973 May;133(1):165-71. doi: 10.1042/bj1330165.
5
The effect of modifying lysine-126 on the physical, catalytic and regulatory properties of bovine liver glutamate dehydrogenase.修饰赖氨酸-126对牛肝谷氨酸脱氢酶物理、催化及调节特性的影响
Biochem J. 1973 May;133(1):173-82. doi: 10.1042/bj1330173.
6
The role of histidine residues in glutamate dehydrogenase.组氨酸残基在谷氨酸脱氢酶中的作用。
Biochem J. 1972 Sep;129(2):419-25. doi: 10.1042/bj1290419.
7
The inhibition of glutamate dehydrogenase by L-serine O-sulphate and related compounds and by photo-oxidation in the presence of Rose Bengal.L-丝氨酸O-硫酸酯及相关化合物以及在孟加拉玫瑰红存在下通过光氧化对谷氨酸脱氢酶的抑制作用。
Biochem J. 1971 Jul;123(3):421-6. doi: 10.1042/bj1230421.
8
Inactivation of the rabbit parotid Na/K/Cl cotransporter by N-ethylmaleimide.N-乙基马来酰亚胺对兔腮腺钠/钾/氯协同转运体的失活作用。
J Membr Biol. 1989 Nov;112(1):51-8. doi: 10.1007/BF01871163.
9
The equilibrium position of the reaction of bovine liver glutamate dehydrogenase with pyridoxal5'-phosphate. A demonstration that covalent modification with this reagent completely abolishes catalytic activity.牛肝谷氨酸脱氢酶与磷酸吡哆醛反应的平衡位置。证明用该试剂进行共价修饰会完全消除催化活性。
Biochem J. 1975 May;147(2):351-8. doi: 10.1042/bj1470351.
10
The equilibrium assumption is valid for the kinetic treatment of most time-dependent protein-modification reactions.平衡假设对于大多数随时间变化的蛋白质修饰反应的动力学处理是有效的。
Biochem J. 1979 Sep 1;181(3):775-8. doi: 10.1042/bj1810775.