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008			130917s2013 xxu| s |||| 0|eng d
020			_a9781461486664 _9978-1-4614-8666-4
024	7		_a10.1007/978-1-4614-8666-4 _2doi
050		4	_aR-RZ
072		7	_aMBGR _2bicssc
072		7	_aMED000000 _2bisacsh
082	0	4	_a610 _223
100	1		_aKinter, Michael. _eauthor.
245	1	0	_aApplication of Selected Reaction Monitoring to Highly Multiplexed Targeted Quantitative Proteomics _h[electronic resource] : _bA Replacement for Western Blot Analysis / _cby Michael Kinter, Caroline S. Kinter.
264		1	_aNew York, NY : _bSpringer New York : _bImprint: Springer, _c2013.
300			_aXIII, 65 p. 14 illus., 11 illus. in color. _bonline resource.
336			_atext _btxt _2rdacontent
337			_acomputer _bc _2rdamedia
338			_aonline resource _bcr _2rdacarrier
347			_atext file _bPDF _2rda
490	1		_aSpringerBriefs in Systems Biology, _x2193-4746
505	0		_aThe use of mass spectrometry for highly selective detection -- overview of how the selected reaction monitoring experiment works -- Designing a selected reaction monitoring method for a protein -- Example analyses include: sample processing, sample analysis, data processing -- Future Directions.
520			_a  A key experiment in biomedical research is monitoring the expression of different proteins in order to detect changes that occur in biological systems under different experimental conditions.  The method that is most widely used is the Western blot analysis.  While Western blot is a workhorse in laboratories studying protein expression and has several advantages, it also has a number of significant limitations.  In particular, the method is semi-quantitative with limited dynamic range.  Western blot focuses on a single protein per sample with only a small number of representative samples analyzed in an experiment.  New quantitative tools have been needed for some time to at least supplement, & possibly replace, the Western blot. Mass spectrometric methods have begun to compete with Western blot for routine quantitative analyses of proteins.  One of these methods is based on the tandem mass spectrometry technique of selected reaction monitoring (SRM), which is also called multiple reaction monitoring (MRM).  Selected reaction monitoring is actually an older tandem mass spectrometry technique, first described in the late 70s, that is widely utilized in the quantitative analysis of small molecules like drugs & metabolites.  The use of selected reaction monitoring for the quantitative analysis of proteins has a number of advantages.  Most importantly, it is fundamentally quantitative with a wide dynamic range.  The output of the analysis is a numerical result that can range over several orders of magnitude.  Other advantages include sufficient specificity & sensitivity to detect low abundance proteins in complex mixtures.  Finally, selected reaction monitoring can be multiplexed to allow the quantitative analysis of relatively large numbers of proteins in a single sample in a single experiment.     This Brief will explain both the theoretical & experimental details of the selected reaction monitoring experiment as it is applied to proteins.
650		0	_aMedicine.
650		0	_aMass spectrometry.
650		0	_aBiochemistry.
650		0	_aProteomics.
650	1	4	_aBiomedicine.
650	2	4	_aBiomedicine general.
650	2	4	_aProteomics.
650	2	4	_aMass Spectrometry.
650	2	4	_aBiochemistry, general.
700	1		_aKinter, Caroline S. _eauthor.
710	2		_aSpringerLink (Online service)
773	0		_tSpringer eBooks
776	0	8	_iPrinted edition: _z9781461486657
830		0	_aSpringerBriefs in Systems Biology, _x2193-4746
856	4	0	_uhttp://dx.doi.org/10.1007/978-1-4614-8666-4
912			_aZDB-2-SBL
942			_2Dewey Decimal Classification _ceBooks
999			_c45042 _d45042