Abstract
A high throughput process including subcellular fractionation and multiple protein separation and identification technology allowed us to establish the protein expression profile of human fetal liver, which was composed of at least 2,495 distinct proteins and 568 non-isoform groups identified from 64,960 peptides and 24,454 distinct peptides. In addition to the basic protein identification mentioned above, the MS data were used for complementary identification and novel protein mining. By doing the analysis with integrated protein, expressed sequence tag, and genome datasets, 223 proteins and 15 peptides were complementarily identified with high quality MS/MS data.
Highlights
A high throughput process including subcellular fractionation and multiple protein separation and identification technology allowed us to establish the protein expression profile of human fetal liver, which was composed of at least 2,495 distinct proteins and 568 non-isoform groups identified from 64,960 peptides and 24,454 distinct peptides
Between weeks 16 and 24 of gestation the human fetal liver (HFL)[1] is a major site of fetal hematopoiesis and is at the critical turning point between immigration and emigration of the hematopoietic system (1)
Liver samples were immediately washed completely with iced PBS at 4 °C, and a portion of the samples was preserved in liquid nitrogen until use; the rest was used for subcellular fractionation
Summary
Chinese volunteers underwent induction of labor by breaking with water bag in Beijing Northern Taiping Road Hospital. From the ‡Department of Genomics and Proteomics, Beijing Institute of Radiation Medicine, Beijing Proteomics Research Center, 27 Taiping Road, Beijing 100850, China, §Beijing Proteome Research Center, 33 Life Garden Road, Beijing 102206, China, and ʈInstitutes of Biomedical Sciences, Fudan University, Shanghai 200032, China. Weeks were used for proteomic analysis after obtaining informed consent. Liver samples were immediately washed completely with iced PBS at 4 °C, and a portion of the samples was preserved in liquid nitrogen until use; the rest was used for subcellular fractionation. For the subcellular proteome analysis, nuclei, mitochondria, plasma membrane (PM), and cytosol were fractionated according to the procedure described by Fleischer and Kervina (2) with minor modifications. The purity and enrichment for fractionated organelles were determined by electron micrograph and enzyme marker assay and specific immunoblotting, respectively (Supplemental Fig. S1). (For details see the supplemental materials and methods.)
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