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Purine excretion by mammalian cells deficient in adenosine kinase
Author(s) -
Chan TehSheng,
Ishii Kazuhiro,
Long Cedric,
Green Howard
Publication year - 1973
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1040810304
Subject(s) - hypoxanthine , adenosine kinase , adenosine , purine metabolism , xanthine , purine , biochemistry , mutant , hypoxanthine guanine phosphoribosyltransferase , guanine , biology , inosine , chemistry , cell culture , microbiology and biotechnology , adenosine deaminase , enzyme , nucleotide , genetics , gene
An adenosine kinaseless (AK − ) mutant of the mouse fibroblast line 3T6 has been obtained in cell culture by evolution of resistance to 6‐thio‐methylpurine ribonucleoside and tubercidin. The mutant excretes purines (xanthine and hypoxanthine) into the culture medium. Human or mouse cells lacking hypoxanthine‐guanine phosphoribosyl transferase (HPT − ) excrete increased amounts of purines, but a human cell mutant lacking both HPT and AK excretes considerably more hypoxanthine. The difference in hypoxanthine excretion between the HPT − mutant and the HPT − AK − mutant originates from the adenosine normally reutilized through the activity of adenosine kinase. The activity of adenosine kinase is essential to retard the adenosine cycle and to prevent cellular loss of purines.