Nature Biotechnology
21, 281 - 286 (2003)
Published online: 18 February 2003; | doi:10.1038/nbt793
Characterization of the human heart mitochondrial proteomeSteven W. Taylor1, Eoin Fahy1, Bing Zhang1, Gary M. Glenn1, Dale E. Warnock1, Sandra Wiley1, Anne N. Murphy1, Sara P. Gaucher2, Roderick A. Capaldi3, Bradford W. Gibson2
& Soumitra S. Ghosh11
MitoKor, 11494 Sorrento Valley
Road, San Diego, California
92121. 2
Buck Institute for Age Research,
Novato, California 94945. 3
Institute for Molecular Biology, University of
Oregon, Eugene, Oregon 97403.
Correspondence should be addressed to Steven W. Taylor
taylors@mitokor.comTo gain a better understanding of the critical role of mitochondria
in cell function, we have compiled an extensive catalogue of the mitochondrial
proteome using highly purified mitochondria from normal human heart tissue.
Sucrose gradient centrifugation was employed to partially resolve protein
complexes whose individual protein components were separated by one-dimensional
PAGE. Total in-gel processing and subsequent detection by mass spectrometry and
rigorous bioinformatic analysis yielded a total of 615 distinct protein
identifications. All protein pI values, molecular weight ranges, and
hydrophobicities were represented. The coverage of the known subunits of the
oxidative phosphorylation machinery within the inner mitochondrial membrane was
>90%. A significant proportion of identified proteins are involved in
signaling, RNA, DNA, and protein synthesis, ion transport, and lipid
metabolism. The biochemical roles of 19% of the identified proteins have not
been defined. This database of proteins provides a comprehensive resource for
the discovery of novel mitochondrial functions and pathways.
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