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- W2091784954 abstract "Presteady state kinetics of the interaction of lysozyme with the hexamer and trimer of N-acetylglucosamine have been investigated by stopped-flow and relaxation methods. Two processes were observed with hexamer, and only one with trimer. The processes for hexamer were observed either as two consecutive proton uptake signals or as a fast increase followed by a slower decrease in fluorescence intensity. The faster of the two processes is identical to the process observed when trimer binds to the unproductive ABC sites of lysozyme. The slower of the two processes is presumably associated with the productive binding of hexamer with the enzyme." @default.
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- W2091784954 date "1970-07-01" @default.
- W2091784954 modified "2023-09-26" @default.
- W2091784954 title "Kinetics of lysozyme-substrate interactions" @default.
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- W2091784954 doi "https://doi.org/10.1016/0006-291x(70)91061-2" @default.
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