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A DNA two-dimensional electrophoresis system was used to obtain digital maps of the proteins of human blood neutrophils. The proteins of the neutrophils were resolved on a 0.84% agarose gel and visualized by use of Coomassie blue staining. Protein spots of interest were excised, digested in-gel, and analyzed by microcapillary reversed-phase liquid chromatography-electrospray tandem mass spectrometry. Twenty-seven proteins were identified, including five actin isoforms, seven other structural proteins, six kinases, two enzymes, and two unknowns. Although quantitative differences in protein abundance in the neutrophils were not identified, several proteins identified in the smear were revealed to be significantly more abundant in the nucleus. These included DNA topoisomerase II and spectrin alpha I. This technique was also used to demonstrate the presence of actin in the plasma membrane of mouse, rat, and bovine polymorphonuclear leukocytes. This study demonstrates the feasibility of a multiplexed protein sequencing method for the identification of proteins of intracellular compartments using 2D gels and mass spectrometry.City school board members debated whether to move forward on changing membership requirements or to “consider a moratorium” until all stakeholders could be heard at a


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