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Optical and chemical identification of kinetic steps in trypsin- and chymotrypsin-catalysed reactions

Previous interpretations of the mechanism of trypsin- and chymotrypsin-catalysed reactions in terms of two intermediates, the Michaelis complex and an acyl-enzyme, were based on steady-state studies and on the observation of individual steps under sub-optimum conditions. In the present paper new met...

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Detalles Bibliográficos
Autores principales: Barman, T. E., Gutfreund, H.
Formato: Artigo
Lenguaje:Inglês
Publicado: 1966
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Acceso en línea:https://ncbi.nlm.nih.gov/pmc/articles/PMC1270122/
https://ncbi.nlm.nih.gov/pubmed/5966278
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