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10.1021/ac400761e http://scihub22266oqcxt.onion/10.1021/ac400761e C3696186!3696186!23688297     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Anal+Chem 2013 ; 85 (11): 5555-61 Nephropedia Template TP {{tp|p=23688297|t=2013. Glycomic analysis using glycoprotein immobilization for glycan extraction |pdf=|usr=}}{{23688297}} gab.com Text Glycomic analysis using glycoprotein immobilization for glycan extraction JO: Anal Chem http://www.kidney.de/pget.php?&tw=1&pmid=23688297 #FOAvip Glycosylation is one of the most common protein modifications and is involved in many functions of glycoproteins. Investigating aberrant protein glycosylation associated with diseases is useful in improving disease diagnostics. Due to the non-template nature of glycan biosynthesis, the glycans attached to glycoproteins are enormously complex; thus, a method for comprehensive analysis of glycans from biological or clinical samples is needed. Here, we describe a novel method for glycomic analysis using glycoprotein Immobilization for glycan extraction (GIG). Proteins or peptides from complex samples were first immobilized on solid support, and other non-conjugated molecules were removed. Glycans were enzymatically or chemically modified on solid-phase before releasing from glycoproteins/glycopeptides for mass spectrometry analysis. The method was applied to the glycomic analysis of both N- and O-glycans. Twit Text FOAVip Glycomic analysis using glycoprotein immobilization for glycan extraction ????Anal Chem http://www.kidney.de/pget.php?&tw=1&pmid=23688297 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=23688297 #FOAvip English Wikipedia <ref>{{Cite pmid|23688297}}</ref> Glycomic analysis using glycoprotein immobilization for glycan extraction #MMPMID23688297 Yang S; Li Y; Shah P; Zhang H Anal Chem 2013[Jun]; 85 (11): 5555-61 PMID23688297show ga Glycosylation is one of the most common protein modifications and is involved in many functions of glycoproteins. Investigating aberrant protein glycosylation associated with diseases is useful in improving disease diagnostics. Due to the non-template nature of glycan biosynthesis, the glycans attached to glycoproteins are enormously complex; thus, a method for comprehensive analysis of glycans from biological or clinical samples is needed. Here, we describe a novel method for glycomic analysis using glycoprotein Immobilization for glycan extraction (GIG). Proteins or peptides from complex samples were first immobilized on solid support, and other non-conjugated molecules were removed. Glycans were enzymatically or chemically modified on solid-phase before releasing from glycoproteins/glycopeptides for mass spectrometry analysis. The method was applied to the glycomic analysis of both N- and O-glycans. äGlycomic analysis using glycoprotein immobilization for glycan extract(epmc).pdf DeepDyve Pubget Overpricing