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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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Библиографические подробности
Главные авторы: Shaw, W. H., Anderson, J. W.
Формат: Artigo
Язык:Inglês
Опубликовано: 1972
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Online-ссылка:https://ncbi.nlm.nih.gov/pmc/articles/PMC1178578/
https://ncbi.nlm.nih.gov/pubmed/5073745
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