Profiling Kinase Activities by Using a Peptide Chip and Mass Spectrometry
β Scribed by Dal-Hee Min; Jing Su; Milan Mrksich
- Publisher
- John Wiley and Sons
- Year
- 2004
- Tongue
- English
- Weight
- 210 KB
- Volume
- 116
- Category
- Article
- ISSN
- 0044-8249
No coin nor oath required. For personal study only.
β¦ Synopsis
Herein we describe a strategy that combines peptide chips with matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry (MS) to evaluate kinase activities rapidly and semi-quantitatively. We have already shown that monolayers of alkanethiolates on gold are wellsuited as substrates for MALDI-TOF MS, and could be used to measure enzyme activities and to perform high-throughput screenings. [1,2] A significant aspect of this approach-which we term SAMDI (self-assembled monolayers for MALDI) MS-is that it avoids the use of labels, greatly simplifying the formatting of assays. Herein we establish two important
π SIMILAR VOLUMES
Phenolic and catecholamine polymers are common constituents of many biological systems. Cross-linking of polyphenols with other phenols, peptides, proteins and carbohydrates results in the synthesis of complex natural products which are not easily characterized. Electrospray mass spectrometry (ES-MS
Synthetic proteins with unusual architecture are obtained through chemoselective ligation, a method based on the condensation of unprotected peptides under mild aqueous conditions. The last step of a new procedure leading to a tri-branched conjugate consists of the chemoselective ligation reaction b
The combination of capillary electrophoresis with mass spectrometry allows efficient separation and identification of components in mixtures with greater specificity than can be obtained using capillary electrophoresis and ultra violet detection alone. For the mixture of peptides analysed in this ap