Stopped-flow cryoenzymological investigation of the pre-steady-state kinetics of hydrolysis of Leu-Gly-NHNH-Dns by leucine aminopeptidase.
Stopped-flow cryoenzymological investigation of the pre-steady-state kinetics of hydrolysis of Leu-Gly-NHNH-Dns by leucine aminopeptidase.
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亮氨酸氨基肽酶水解 Leu-Gly-NHNH-Dns 的前稳态动力学的停流冷冻酶学研究。
DOI：
10.1021/bi00414a018
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发表时间：
1988
期刊：
影响因子：
2.9
通讯作者：
VanWart,HE
中科院分区：
文献类型：
--
作者：
Lin,WY;Lin,SH;Morris,RJ;VanWart,HE
Materials and Methods Materials. The source and purification of the LAP, and other materials and the synthesis of Leu-Gly-NHNH-Dns have been described elsewhere (Lin & Van Wart, 1988a, b; Lin et al., 1988). Leu-NHOH was purchased from Sigma Chemical Co. Reagent-grade methanol was purchased from Mallinck-rodt.Measurement of pH* and Preparation of Solutions. The apparent protonjc activity in aqueous-organic solutions, pH*, was measured by using an Oreil Model 611 pH meter with a Ross Model 8103 combination glass electrode as described by Fink andGeeves (1979). To prepare a solution with the desired pH* at a subzero temperaturein a given buffer and cryosolvent, tables of the temperature dependence of pH*(Douzou, 1977) were used to estimate the change in pH* expected on lowering the temperature from 1
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