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Adenosine deaminase from deoxycoformycin-sensitive and -resistant rat hepatoma cells. Purification and characterization.

Authors: Hunt SW, 3RD  Hoffee, PA 
Citation: Hunt SW 3rd and Hoffee PA, J Biol Chem. 1982 Dec 10;257(23):14239-44.
Pubmed: (View Article at PubMed) PMID:6815190

Deoxycoformycin-resistant rat hepatoma cells exhibit up to 300-fold increase in adenosine deaminase activity compared to the sensitive parental cells. In order to determine the basis of the increased enzyme activity in deoxycoformycin-resistant cells, adenosine deaminase was purified from rat liver and deoxycoformycin-sensitive and -resistant cells. Physical, kinetic, and immunological properties of the purified enzymes were compared. Purified adenosine deaminase from all sources was found to be a monomer with an Mr approximately 45,000. In addition, the purified enzymes had a similar isozyme pattern in nondenaturing polyacrylamide gels. Km values for adenosine and Ki values for deoxycoformycin did not differ among the purified enzymes. By double diffusion analysis and quantitative immunoprecipitation, the purified enzymes were found to be immunologically indistinguishable. These data indicate that deoxycoformycin-resistant rat hepatoma cells produce increased amounts of adenosine deaminase protein which results in increased enzymatic activity.


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CRRD Object Information
CRRD ID: 2291855
Created: 2008-04-01
Species: All species
Last Modified: 2008-04-01
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.