Abstract
Adenosine 5' monophosphate is dephosphorylated before its uptake by cells of E. coli. This is demonstrated by using a radioactive double labeled culture, and with a 5' nucleotidase deficient mutant strain. The adenosine formed is further phosphorylated to adenine as a prerequisite for its uptake and incorporation. The cellular localization of the enzymes involved in the catabolism of adenosine 5' monophosphate is discussed.
Original language | English |
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Pages (from-to) | 401-405 |
Number of pages | 5 |
Journal | Journal of Bacteriology |
Volume | 121 |
Issue number | 2 |
State | Published - 1975 |