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Purification, properties and substrate specificity of adenosine triphosphate sulphurylase from spinach leaf tissue
1. ATP sulphurylase was purified up to 1000-fold from spinach leaf tissue. Activity was measured by sulphate-dependent [(32)P]PP(i)–ATP exchange. The enzyme was separated from Mg(2+)-requiring alkaline pyrophosphatase (which interferes with the PP(i)–ATP-exchange assay) and from other PP(i)–ATP-exch...
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| Главные авторы: | , |
|---|---|
| Формат: | Artigo |
| Язык: | Inglês |
| Опубликовано: |
1972
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| Предметы: | |
| Online-ссылка: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1178578/ https://ncbi.nlm.nih.gov/pubmed/5073745 |
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