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Purification and steady-state kinetics of adenosine 5'-pyrophosphate sulphurylase from baker's yeast.
ADP sulphurylase (EC 2.7.7.5) was purified by chromatography on Sephadex G-200 and DEAE-cellulose. The enzyme was assayed by measuring the incorporation of [32P]Pi into ADP in the presence of the substrate for the reverse reaction, adenosine 5'-sulphatophosphate. In the concentration ranges inv...
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| Format: | Artigo |
| Langue: | Inglês |
| Publié: |
1977
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| Sujets: | |
| Accès en ligne: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1164880/ https://ncbi.nlm.nih.gov/pubmed/329837 |
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