PMF typically involves elaborate sample preparation. A protein mixture is spread across a gel and separated into individual proteins, which are scooped out of the gel and cut with protein scissors into predictable, small pieces called peptides. The samples are then analyzed using matrix-assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF MS), which identifies protein fragments based on the time they need to travel a defined distance when being accelerated in a vacuum.
In their study, Rolf U. Halden, PhD, PE, assistant professor in the Department of Environmental Health Sciences Bloomberg School of Public Health and his colleagues demonstrate how PMF and mass spectrometry are used to identify a unique dioxin-degrading enzyme in a soup of hundreds of cell proteins. The technique avoids elaborate conventional sample preparation steps by coaxing the cells into mass production of the protein the researchers wish to analyze.
"Finding a specific target in a mixture of hundreds of proteins can be likened to finding the proverbial needle in the haystack; this task can be performed much faster and more economically if you have more needles--and that's exactly what our method
Source:Johns Hopkins University Bloomberg School of Public Health