溶解度
硫酸铵
盐析
化学
盐(化学)
离子强度
降水
腌制
铵
无机化学
分子
离子
溶解
蛋白质沉淀
硫酸铵沉淀
色谱法
水溶液
生物化学
有机化学
食品科学
大小排阻色谱法
萃取(化学)
酶
气象学
物理
作者
Krisna C. Duong‐Ly,Sandra B. Gabelli
出处
期刊:Methods in Enzymology
日期:2014-01-01
卷期号:: 85-94
被引量:204
标识
DOI:10.1016/b978-0-12-420119-4.00007-0
摘要
Protein solubility is affected by ions. At low ion concentrations (<0.5 M), protein solubility increases along with ionic strength. Ions in the solution shield protein molecules from the charge of other protein molecules in what is known as 'salting-in'. At a very high ionic strength, protein solubility decreases as ionic strength increases in the process known as 'salting-out'. Thus, salting out can be used to separate proteins based on their solubility in the presence of a high concentration of salt. In this protocol, ammonium sulfate will be added incrementally to an E. coli cell lysate to isolate a recombinantly over-expressed protein of 20 kDa containing no cysteine residues or tags.
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