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The in vitro effect of adenine on pyruvate kinase‐deficient red cells
Author(s) -
Lappin T. R. J.,
Elder G. E.,
Savage G. A.,
Cooke P. J.,
Bridges J. M.
Publication year - 1982
Publication title -
british journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.907
H-Index - 186
eISSN - 1365-2141
pISSN - 0007-1048
DOI - 10.1111/j.1365-2141.1982.tb07291.x
Subject(s) - adenine nucleotide , haemolysis , pyruvate kinase , biochemistry , incubation , oxidative phosphorylation , adenosine triphosphate , nucleotide , mitochondrion , atp–adp translocase , phosphorylation , chemistry , biology , metabolism , microbiology and biotechnology , glycolysis , inner mitochondrial membrane , immunology , gene
In pyruvate kinase (PK)‐deficient blood with high levels of reticulocytes, the degree of haemolysis after incubation at 37°C for 48 h was halved by the inclusion of adenine in the medium. The decrease in haemolysis was associated with a higher ATP level but was not related to the pH of the incubation mixture. The incorporation of adenine into nucleotides studied over a 3 h period was similar in normal and PK‐deficient blood. The observed increase in cellular ATP was equivalent to that shown by radioactive measurements to have been synthesized from added adenine. Inhibition of mitochondrial oxidative phosphorylation in the reticulocytes of the PK‐deficient blood by KCN reduced the amount of adenine taken up by the cells by a factor of 3 and altered the pattern of incorporation into the nucleotides. Only 25% of the adenine which entered the blood cells was converted into ATP compared with 85% in the absence of cyanide. Despite the synthesis of small amounts of ATP from labelled adenine, the overall ATP content fell to less than 50% of its original level. It is suggested that incubation with adenine increased the ATP level in the reticulocytes by virtue of mitochondrial oxidative phosphorylation thereby reducing the haemolysis of these cells.