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- W954380849 abstract "Publisher Summary This chapter discusses the methodology of adenylosuccinate synthetase assay. Adenylosuccinate synthetase preparations with varying degrees of purity are obtained from cell-free extracts of Escherichia coli , Bacillissubtilis , Schizosaccharomyces pombe , wheat germ, Ehrlich ascites tumor cells, Novikoff ascites tumor cells, and human placenta. The adenylosuccinate produced is assayed by recording the initial rate of absorbance change at 280 nm, as the 6 position of the purine ring is N-substituted. The assay is carried out at room temperature (22°) at pH 7.0 (about the pH maximum for the enzyme activity). The spectrophotometric assay may be sensitive to stray light effects that are dependent on the quality of the optical system of the spectrophotometer and the respective range of absorption. This becomes, especially important for inhibition studies with purine derivatives that absorb in the 280 nm region. Although the inhibitory mechanism is uncertain, these anions tend to be the competitive inhibitors of guanosine triphosphate (GTP) binding. Acetate salts of buffers and reagents should be used in the reaction mixtures to avoid complications in kinetic or binding investigations." @default.
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- W954380849 date "1978-01-01" @default.
- W954380849 modified "2023-09-23" @default.
- W954380849 title "[27] Adenylosuccinate synthetase (rabiit muscle, heart, and liver)" @default.
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- W954380849 doi "https://doi.org/10.1016/s0076-6879(78)51029-x" @default.
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