首页> 外文期刊>Biochimica et Biophysica Acta. Protein Structure and Molecular Enzymology >Water sorption isotherms and enthalpies of water sorption by lysozyme using the quartz crystal microbalance/heat conduction calorimeter
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Water sorption isotherms and enthalpies of water sorption by lysozyme using the quartz crystal microbalance/heat conduction calorimeter

机译:石英晶体微量天平/热传导量热仪的吸水等温线和溶菌酶的吸水焓

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摘要

The water sorption isotherm and the water vapor activity dependence of the enthalpy of water sorption △_(sorp)H° of lysozyme have been measured at 25 ℃. A thin film of lysozyme of mass 250 μg was exposed to H_2O/N_2 mixtures in a quartz crystal microbalance/heat conduction calorimeter (QCM/HCC). The QCM/HCC is a new gravimetric/calorimetric method that measures simultaneously and with high precision the mass change and the corresponding heat flow in a thin film exposed to a gas. △_(sorp)H250L鉬or lysozyme agrees with previous determinations, although hysteresis effects are evident in the data. No van't Hoff analysis is necessary because sorption enthalpies are measured calorimetrically. The water vapor activity dependence of △_(sorp)H°agrees with that measured previously by Bone. As the water content of the lysozyme film drops below 10 mass%, △_(sorp)H°becomes more exothermic, indicating that water is being bound to the charged or highly polar groups of the solvent-accessible surface of lysozyme. The dynamics of water uptake and release from lysozyme thin films are much slower than in polymer films of comparable thickness. Because the QCM/HCC operates with sub--milligram samples, any protein is now amenable to study by this technique.
机译:在25℃下测定了溶菌酶的吸水等温线和吸水焓△_(sorp)H°的水蒸气活度依赖性。将质量为250μg的溶菌酶薄膜暴露在石英微天平/热导热量计(QCM / HCC)中的H_2O / N_2混合物中。 QCM / HCC是一种新的重量/量热方法,可以同时高精度地测量暴露于气体的薄膜中的质量变化和相应的热流。 △_(sorp)H250LMo或溶菌酶与先前的测定结果一致,尽管在数据中有明显的滞后效应。不需要进行Van't Hoff分析,因为吸附焓是通过量热法测量的。 △_(sorp)H°的水蒸气活度依赖性与先前由Bone测量的水蒸气活度依赖性一致。当溶菌酶膜的水含量降至10质量%以下时,△_(sorp)H°变得更放热,表明水与溶菌酶的溶剂可及表面的带电或高极性基团结合。溶菌酶薄膜的吸水和释放动力学要比具有相同厚度的聚合物薄膜慢得多。由于QCM / HCC可处理亚毫克样品,因此现在可以使用此技术研究任何蛋白质。

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