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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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Hlavní autoři: Barman, T. E., Gutfreund, H.
Médium: Artigo
Jazyk:Inglês
Vydáno: 1966
Témata:
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC1270122/
https://ncbi.nlm.nih.gov/pubmed/5966278
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