A method for deriving kinetic constants for two enzymes acting on the same substrate.
作者信息
Spears G, Sneyd J G, Loten E G
出版信息
Biochem J. 1971 Dec;125(4):1149-51. doi: 10.1042/bj1251149.
Abstract
摘要
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A method for deriving kinetic constants for two enzymes acting on the same substrate.
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本文引用的文献
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Negative cooperativity in regulatory enzymes.
Proc Natl Acad Sci U S A. 1969 Apr;62(4):1121-8. doi: 10.1073/pnas.62.4.1121.
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An effect of insulin on adipose-tissue adenosine 3':5'-cyclic monophosphate phosphodiesterase.
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Multiple cyclic nucleotide phosphodiesterase activities from rat brain.
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Hydrolysis of cyclic guanosine and adenosine 3',5'-monophosphates by rat and bovine tissues.
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Effects of guanosine 3',5'-monophosphate on glycerol production and accumulation of adenosine 3',5'-monophosphate by fat cells.
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The assay of adenosine 3',5'-cyclic monophosphate and guanosine 3',5'-cyclic monophosphate in biological materials by enzymatic radioisotopic displacement.
Biochemistry. 1968 Dec;7(12):4177-81. doi: 10.1021/bi00852a006.
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[Influence of hydrochlorothiazide and other sulfamoyl diuretics on the activity of 3',5'-AMP phosphodiesterase in rat kidney].
Naunyn Schmiedebergs Arch Exp Pathol Pharmakol. 1968;259(4):344-59.
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