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- W1844296940 abstract "This chapter describes the methodology of purification of adenine phosphoribosyltransferase from rat liver. All steps in the purification are carried out at 2–4°, and all solutions contain 5 mM mercaptoethanol, unless stated otherwise. Adenine phosphoribosyltransferase has been purified in reasonable yield from several mammalian tissues. The rat liver enzyme possesses unusual “initial burst” kinetics in that a rapid limited synthesis of adenosine monophosphate (AMP) is followed by a sustained steady-state synthesis of AMP. When the liver enzyme is purified to apparent homogeneity, the two reaction phases of AMP synthesis are found to be catalyzed by the same protein molecule. Adenine phosphoribosyltransferase converts adenine into AMP using PP-ribose-P as cosubstrate. It is usually necessary to purify the commercial preparations of radioactive adenine to reduce the content of radiation self-decomposition products that are not extractable by butanol." @default.
- W1844296940 created "2016-06-24" @default.
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- W1844296940 date "1978-01-01" @default.
- W1844296940 modified "2023-09-26" @default.
- W1844296940 title "[79] Adenine phosphoribosyltransferase from rat liver" @default.
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- W1844296940 doi "https://doi.org/10.1016/s0076-6879(78)51080-x" @default.
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