Kinetics of 5-aza-2'-deoxycytidine phosphorylation in mouse spleen and L1210 leukemic cell extracts.

Abstract:

:Out of different nucleosides and deoxynucleosides testes for their ability to block the phosphorylation of labeled 5-aza-2'-deoxycytidine in the presence of ATP and the cell-free extract from mouse spleen only deoxycytidine and cytosine arabinoside depressed the reaction significantly. With the same system the phosphate donor specificity for 5-aza-2'-deoxycytidine and deoxycytidine was determined. All of the 5'-triphosphates used were less efficient donors with respect to the analogue than to the natural substrate. The apparent Michaelis constants for the phosphorylation of 5-aza-2'-deoxycytidine and deoxycytidine were 2.9 and 2.5 x 10(-5) M, respectively. Using the extract from L1210 leukemic cells the Km constant for 5-aza-2'-deoxycytidine was 6.4 x 10(-5) M and that for deoxycytidine 2.7 x 10(-5) M. The Ki constants with the spleen extract were 1.2 x 10(-3) M for 5-aza-2'-deoxycytidine and 5.8 x 10(-6) M for deoxycytidine. Both compounds acted as competitive inhibitors of one another.

journal_name

Neoplasma

journal_title

Neoplasma

authors

Veselý J,Cihák A

subject

Has Abstract

pub_date

1980-01-01 00:00:00

pages

121-7

issue

2

eissn

0028-2685

issn

1338-4317

journal_volume

27

pub_type

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