Protein Purification Principles And Trends [Paperback]

Chapter 1 uses SILAC and TMT quantitative MS methods to identify novel target proteins modulated in the erlotinib (EGFR TKI) resistant lung cancer cells. The use of multiplex quantitative proteomic strategies, such as SILAC and TMT protein labeling are powerful methods for identifying a large number of novel biomarkers.

Chapter 2 describes a MALDI-TOF/TOF based proteomic approach to profile HAPE-related proteomic changes in plasma. 25 differential plasma proteins responsible for the discrimination between the two groups from HAPE subjects and healthy controls have been identified and studied based on their biological functions. Furthermore, two of the 25 proteins (Haptoglobin and Apoliprotein A- I) have been considered as putative biomarkers for HAPE.

Chapter 3 discusses an important oxidative stress-mediated tyrosine nitration in a protein in tumorigenesis, and addresses the principles of nitroproteomics, isolation and purification of nitroproteins, mass spectrometry characteristics of nitropeptides, methodology used for nitroproteomics in pituitary adenomas, current status of human pituitary nitroproteomics studies, and future trends.

Chapter 4 introduces the fabrication process of boron nitride nanopores and demonstrates the conductance change in ionic current due to the translocation of both dsDNA and ssDNA through the nanopore. It open a window for DNA sensing with boron nitride nanopores and a potential platform for future DNA sequencing application.

Chapter 5 shows the purification of fission yeast Dmc1 and its accessory proteins, and describes a conventional method to monitor DNA strand exchange reaction, which is a powerful tool to understand the biological significance of Dmc1 as well as its accessory proteins.

Chapter 6 aims to detail with necessary basic methods in protein purification and analysis that leads us to grasp new roles assigned to the $\alpha$1--$\beta$2 (and $\alpha$2--$\beta$1) interface of the human hlS„