Kinetic behaviour and allosteric regulation of human deoxycytidylate deaminase derived from leukemic cells

Deoxycytidylate deaminase has been highly purified (1232-fold) from human leukemia CCRF-CEM cells. The native molecular weight of the enzyme is 108 000 and subunit molecular weight 50 500, suggesting that the native enzyme exists as a dimer. The enzyme exhibits a sigmoidal initial velocity vs substr...

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Veröffentlicht in:	Molecular and cellular biochemistry 1983-01, Vol.57 (2), p.185-190
Hauptverfasser:	ELLIMS, P. H, KAO, A. Y, CHABNER, B. A
Format:	Artikel
Sprache:	eng
Schlagworte:	allosteric properties Analytical, structural and metabolic biochemistry Biological and medical sciences Cell Line dCMP deaminase DCMP Deaminase - isolation & purification DCMP Deaminase - metabolism Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Humans Hydrogen-Ion Concentration Hydrolases Kinetics leukemia Leukemia, Lymphoid - enzymology Macromolecular Substances man Molecular Weight Nucleotide Deaminases - metabolism
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