作者: Miki Kikuchi , Naoya Hatano , Sadaki Yokota , Nobuyuki Shimozawa , Tsuneo Imanaka
关键词: Protease 、 Transport protein 、 Gene isoform 、 Cell fractionation 、 Proteomics 、 Biochemistry 、 Biology 、 Peroxisomal targeting signal 、 Cell biology 、 Peroxisome 、 Organelle
摘要: Subcellular proteomics, which includes isolation of subcellular components prior to a proteomic analysis, is advantageous not only in characterizing large macro-molecular complexes such as organelles but also elucidating mechanisms protein transport and organelle biosynthesis. Because the high sensitivity achieved by present proteomics technology, purity samples be analyzed important for interpretation results obtained. In study, peroxisomes isolated from rat liver usual cell fractionation were further purified immunoisolation using specific antibody raised against peroxisomal membrane protein, PMP70. The SDS-PAGE combined with liquid chromatography/mass spectrometry. Altogether 34 known proteins identified addition several mitochondrial microsomal proteins. Some latter may reside well. Analysis fractions all peroxins except Pex7. Two new unknown function abundance. One bi-functional consisting an aminoglycoside phosphotransferase-domain acyl-CoA dehydrogenase domain. other newly peroxisome-specific isoform Lon protease, ATP-dependent protease chaperone-like activity. localization was confirmed immunological techniques. peroxisome-type distinct isoform, play role biogenesis.