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Evidence that Ribulose 1,5-Bisphosphate (RuBP) Binds to Inactive Sites of RuBP Carboxylase in Vivo and an Estimate of the Rate Constant for Dissociation

The binding of ribulose 1,5-bisphosphate (RuBP) to inactive (noncarbamylated) sites of the enzyme RuBP carboxylase in vivo was investigated in Spinacia oleracea and Helianthus annuus. The concentrations of RuBP and inactive sites were determined in leaf tissue as a function of time after a change to...

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Autors principals: Cardon, Zoe G., Mott, Keith A.
Format: Artigo
Idioma:Inglês
Publicat: 1989
Matèries:
Accés en línia:https://ncbi.nlm.nih.gov/pmc/articles/PMC1056004/
https://ncbi.nlm.nih.gov/pubmed/16666692
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