KINETICS OF LYSOZYME-SUBSTRATE INTERACTIONS
KINETICS OF LYSOZYME-SUBSTRATE INTERACTIONS
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DOI：
10.1016/0006-291x(70)91061-2
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发表时间：
1970-01-01
影响因子：
3.1
通讯作者：
HESS, GP
中科院分区：
文献类型：
--
作者：
HOLLER, E;RUPLEY, JA;HESS, GP
本文用停流法和弛豫法研究了溶菌酶与N-乙酰氨基葡萄糖六聚体和三聚体相互作用的前稳态动力学。用六聚体观察到两个过程，而用三聚体仅观察到一个过程。六聚体的过程被观察为两个连续的质子摄取信号或作为一个快速的增加，然后由一个较慢的荧光强度下降。两个过程中较快的过程与三聚体结合到溶菌酶的非生产性ABC位点时观察到的过程相同。这两个过程中较慢的一个可能与六聚体与酶的生产性结合有关。
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.