Proteins by liquid chromatography

J. Bunkenborg, B. J. Pilch, A. V. Podteleinikov, and J. R. Wisniewski, Screening for ZV-glycosylated proteins by liquid chromatography mass spectrometry, ProfeomZcs 4 (2004), 454-465. 

Li, N., Shaw, A.R., Zhang, N.,Mak,A. andLi, L.(2004)Lipidraftproteomics analysis of in-solution digest of sodium dodecyl sulfate-solubilized lipid raft proteins by liquid chromatography-matrix-assisted laser desorption/ionization tandem mass spectrometry. Proteomics 4, 3156-3166. 

Yen TY, Joshi RK, Yan H, Seto NOL, Palcic MM, Macher BA. Characterization of cysteine residues and disulfide bonds in proteins by liquid chromatography/electrospray ionization tandem mass spectrometry. J. Mass Spectrom. 2000 35 990-1002. 

Figure 5.6 Positive-ion electrospray spectrum obtained from the major component in the LC-MS analysis of a purified recombinant 62 kDa protein using a Cig microbore 50 X 1 mm column and a flow rate of 50 p.lmin . The starting buffer (buffer A ) was 0.1% TEA in water, while the gradient buffer (buffer B ) consisted of 0.1% TEA in acetonitrile-water (9 1 vol/vol). The running conditions consisted of 0% B for 5 min, followed by a linear gradient of 100% B for 55 min. Reprinted from J. Chromatogr., B, 685, McAtee, C. P., Zhang, Y., Yarbough, P. O., Fuerst, T. R., Stone, K. L., Samander, S. and Williams, K. R., Purification and characterization of a recombinant hepatitis E protein vaccine candidate by liquid chromatography-mass spectrometry , 91-104, Copyright (1996), with permission from Elsevier Science.

Figure 5.11. Generic approaches to identify interacting proteins within complexes. The complex is isolated from cells by affinity purification using a tag sequence attached to a protein known to be in the complex. Alternatively, the complex can be immunprecipitated with an antibody to one of the proteins in the complex. The proteins are resolved by polyacrylamide gel electrophoresis, proteolyzed, and the mass of the resulting peptides is determined by mass spectrometry. Alternatively, the proteins can be proteolyzed and the resulting peptides resolved by liquid chromatography. The peptide masses are then determined by mass spectrometry and used for database searching to identify the component proteins.

S. G. Allenmark, Separation of enantiomers by protein-based chiral phases in A practical approach to chiral separations by liquid chromatography, G. Subramanian, VCH, Weinheim (1994) Chapter 7. 

Wuhrer, M., Koeleman, C.A., Hokke, C.H., and Deelder, A.M. 2005. Protein glycosylation analysis by liquid chromatography-mass spectrometry. Journal of Chromatography B 825, 124-133. 

M. Ramstrom, I. Ivonin, A. Johansson, H. Askmark, K. E. Markides, R. Zubarev, P. Hakansson, S.-M. Aquilonius, and J. Bergquist. Cerebrospinal Fluid Protein Patterns in Neurodegenerative Disease Revealed by Liquid Chromatography Fourier Transform Ion Cyclotron Resonance Mass Spectrometry. Proteomics, 4(2004) 4010-4018. 

Proteins have also been used as CMPAs for chiral resolution by liquid chromatography. Bovine serum albumin (BSA) and a]-acid glycoproteins (AGP) were investigated as CMPAs. Allenmark et al. [87] used BSA protein as the CMPA for... 

S. A. Carr, M. J. Huddleston, and M. F. Bean, Selective identification and differentiation of N- and O-linked oligosaccharides in glycoproteins by liquid chromatography-mass spectrometry, Protein Sci., 2 (1993) 183-196. 

Biological samples (plasma, serum, blood, and urine) are very complex. They contain a wide variety of matrix components such as proteins, lipids, and salts. To quantify trace amount of analytes (e.g., drug and its metabolites) in complex biological samples by liquid chromatography-mass spectrometry (LC-MS), the samples should be properly treated prior to being injected onto an LC-MS instrument,... 

Quantification of TKIs in patients plasma samples is at present principally performed by liquid chromatography-mass spectrometry (LC-MS) after suitable plasma pretreatment, which implies most generally a protein precipitation with an organic... 

C. F. Harrington, S. Elahi, S. A. Merson, P. Ponnampalavanar, Quantitative analysis of iron-containing protein myoglobin in different foodstuffs by liquid chromatography coupled to high-resolution inductively coupled plasma mass spectrometry, J. AOAC Int., 87 (2004), 253 D258. 

M. A. Palacios, A. Varga, M. Gomez, C. Camara, F. Gavilanes, Evaluation of acid hydrolysis of proteins on Se-aminoacids and trimethylselenonium species by liquid chromatography-microwave digestion-hydride generation-atomic absorption spectrometry, Quim. Anal., 18 (1999), 163-168. 

Microdialysis has also been used as a sampling method for measuring the concentration of drugs in human subcutaneous tissues for pharmacokinetic studies [50]. The microdialysates are simpler than other biological fluids and do not contain proteins, permitting their direct injection for analysis by liquid chromatography. 

---