Measuring enzyme activity in single cells

被引:85
作者
Kovarik, Michelle L. [1 ]
Allbritton, Nancy L. [1 ,2 ,3 ]
机构
[1] Univ N Carolina, Dept Chem, Chapel Hill, NC 27599 USA
[2] Univ N Carolina, Dept Biomed Engn, Chapel Hill, NC 27599 USA
[3] N Carolina State Univ, Raleigh, NC 27695 USA
基金
美国国家卫生研究院;
关键词
CAPILLARY-ELECTROPHORESIS; PROTEOMIC ANALYSIS; ENERGY-TRANSFER; FLOW-CYTOMETRY; CANCER-CELLS; IN-VITRO; ACTIVATION; FLUORESCENCE; METABOLISM; DYNAMICS;
D O I
10.1016/j.tibtech.2011.01.003
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Seemingly identical cells can differ in their biochemical state, function and fate, and this variability plays an increasingly recognized role in organism-level outcomes. Cellular heterogeneity arises in part from variation in enzyme activity, which results from interplay between biological noise and multiple cellular processes. As a result, single-cell assays of enzyme activity, particularly those that measure product formation directly, are crucial. Recent innovations have yielded a range of techniques to obtain these data, including image-, flow- and separation-based assays. Research to date has focused on easy-to-measure glycosylases and clinically-relevant kinases. Expansion of these techniques to a wider range and larger number of enzymes will answer contemporary questions in proteomics and glycomics, specifically with respect to biological noise and cellular heterogeneity.
引用
收藏
页码:222 / 230
页数:9
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