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Catalytic irreversible inhibition of bacterial and plant arginine decarboxylase activities by novel substrate and product analogues.

Arginine decarboxylase (ADC) activity from Escherichia coli and two plant species (oats and barley) was inhibited by five new substrate (arginine) and product (agmatine) analogues. The five compounds, (E)-alpha-monofluoromethyldehydroarginine (delta-MFMA), alpha-monofluoromethylarginine (MFMA), alph...

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Bibliografische gegevens
Hoofdauteurs: Bitonti, A J, Casara, P J, McCann, P P, Bey, P
Formaat: Artigo
Taal:Inglês
Gepubliceerd in: 1987
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Online toegang:https://ncbi.nlm.nih.gov/pmc/articles/PMC1147665/
https://ncbi.nlm.nih.gov/pubmed/3297044
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