Progress curve analysis of adenosine deaminase-catalyzed reactions

作者: Thomas Spector

DOI: 10.1016/0003-2697(84)90796-6

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摘要: Abstract The kinetic constants of the adenosine deaminase-catalyzed conversion to inosine were found be readily obtainable by analyzing progress curve a single reaction. A novel inhibitor, 9-(1-hydroxymethyl-3-methylbutyl)adenine, was studied test validity method with this enzyme. Estimates determined compared those conventional initial velocity analysis. Km and Vmax values for Ki value inhibitor estimated 26.1 μ m , 1.27 μmol/min/unit enzyme, 0.48 respectively, method, 29.3 0.52 shown act competitively substrate both methods experiments very simple perform calculated (with an interfaced microcomputer) within few minutes completion each assay.

参考文章(5)
Thomas Spector, Gerald Hajian, Statistical methods to distinguish competitive, noncompetitive, and uncompetitive enzyme inhibitors Analytical Biochemistry. ,vol. 115, pp. 403- 409 ,(1981) , 10.1016/0003-2697(81)90025-7
Ram P. Agarwal, Thomas Spector, Robert E. Parks, Tight-binding inhibitors-IV. Inhibition of adenosine deaminases by various inhibitors Biochemical Pharmacology. ,vol. 26, pp. 359- 367 ,(1977) , 10.1016/0006-2952(77)90192-7
N O Kaplan, S P Colowick, Jagannathan, M D Joshi, Methods in Enzymology , Vol University Of Nairobi. ,(1966)