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Zhang LJ Wang XE Peng X Wei YJ Cao R Liu Z Xiong JX Yin XF Ping C Liang S 《Cellular and molecular life sciences : CMLS》2006,63(15):1790-1804
To characterize low-copy integral membrane proteins and offer some methods for human liver proteome projects, we fractionated
highly purified rat liver plasma membrane (PM). PM was purified through two sucrose density gradient centrifugations, and
treated with 0.1 M Na2CO3, chloroform/methanol and Triton X-100. Proteins were separated by electrophoresis and submitted to mass spectrometry analysis.
Four hundred and fiftyseven non-redundant membrane proteins were identified, of which 23% (105) were integral membrane proteins
with one or more transmembrane domains. One hundred and fifty-three (33.5%) had no location annotation and 68 were unknown-function
proteins. The proteins from different fractions were complementory. A database search for all identified proteins revealed
that 53 proteins were involved in the cell communication pathway. More interestingly, more than 50% of the proteins had a
protein abundance index concentration of less than 0.1 mol/l, and 12% proteins a concentration 100 times less than that of
arginase 1 and actin.
Received 15 March 2006; received after revision 17 May 2006; accepted 10 June 2006
L.-J. Zhang and X.-e Wang are contributed equally to this work. 相似文献
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The small heat shock proteins and their clients 总被引:11,自引:0,他引:11
Small heat shock proteins are ubiquitous proteins found throughout all kingdoms. One of the most notable features is their
large oligomeric structures with conserved structural organization. It is well documented that small heat shock proteins can
capture unfolding proteins to form stable complexes and prevent their irreversible aggregation. In addition, small heat shock
proteins coaggregate with aggregation-prone proteins for subsequent, efficient disaggregation of the protein aggregates. The
release of substrate proteins from the transient reservoirs, i.e. complexes and aggregates with small heat shock proteins,
and their refolding require cooperation with ATP-dependent chaperone systems. The amphitropic small heat shock proteins were
shown to associate with membranes, although they do not contain transmembrane domains or signal sequences. Recent studies
indicate that small heat shock proteins play an important role in membrane quality control and thereby potentially contribute
to the maintenance of membrane integrity especially under stress conditions.
Received 11 July 2006; received after revision 4 October 2006; accepted 10 November 2006 相似文献
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