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Active-site labelling of triose phosphate isomerase. The reaction of bromohydroxyacetone phosphate with a unique glutamic acid residue and the migration of the label to tyrosine

Triose phosphate isomerase from chicken muscle reacts stoicheiometrically with the active-site-directed irreversible inhibitor bromohydroxyacetone phosphate with concomitant loss of all catalytic activity. The primary site of attachment has been shown to be a unique glutamic acid residue in the sequ...

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Autori principali: De La Mare, Susan, Coulson, A. F. W., Knowles, J. R., Priddle, J. D., Offord, R. E.
Natura: Artigo
Lingua:Inglês
Pubblicazione: 1972
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Accesso online:https://ncbi.nlm.nih.gov/pmc/articles/PMC1174082/
https://ncbi.nlm.nih.gov/pubmed/4643320
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