MECHANISM OF PROTEIN STABILIZATION BY GLYCEROL - PREFERENTIAL HYDRATION IN GLYCEROL-WATER MIXTURES
MECHANISM OF PROTEIN STABILIZATION BY GLYCEROL - PREFERENTIAL HYDRATION IN GLYCEROL-WATER MIXTURES
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DOI：
10.1021/bi00519a023
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发表时间：
1981-01-01
期刊：
影响因子：
2.9
通讯作者：
TIMASHEFF, SN
中科院分区：
文献类型：
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作者：
GEKKO, K;TIMASHEFF, SN
在甘油-水混合物（10-40体积%甘油）中的溶剂组分与7种蛋白质[RNA酶A、牛血清白蛋白、溶菌酶、β-葡聚糖酶、葡聚糖酶、葡聚糖酶、葡聚糖酶、葡聚糖酶]之间的相互作用的密度测定研究。乳球蛋白，胰岛素，α-胰凝乳蛋白酶，胰凝乳蛋白酶原A]在酸性pH区域进行。所有蛋白质在所有使用的条件下优先水合，即，向混合溶剂中加入蛋白质导致甘油的化学势增加。这种化学上不利的相互作用应倾向于使蛋白质和甘油之间的接触表面最小化，并以这种方式稳定球状蛋白质的天然结构。
A densimetric investigation of the interactions between solvent components in glycerol-water mixtures (between 10-40 vol % glycerol) and 7 proteins [RNase A, bovine serum albumin, lysozyme, .beta.-lactoglobulin, insulin, .alpha.-chymotrypsin, chymotrypsinogen A] were carried out in the acid pH region. All the proteins were preferentially hydrated at all conditions used, i.e., addition of the proteins to the mixed solvent results in an increase in the chemical potential of glycerol. This thermodynamically unfavorable interaction should tend to minimize the surface of contact between proteins and glycerol and in this way stabilize the native structure of globular proteins.