From disulfide- to thioether-linked glycoproteins

Angewandte Chemie - International Edition

Volumn 47, Issue 12, 2008, Pages 2244-2247

  Bernardes, Gonçalo J L ^a   Grayson, Elizabeth J ^b   Thompson, Sam ^a   Chalker, Justin M ^a   Errey, James C ^a   El Oualid, Farid ^a   Claridge, Timothy D W ^a   Davis, Benjamin G ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b DURHAM UNIVERSITY   (United Kingdom)

Author keywords

Disulfides; Glycoproteins; Glycosylation; Protein modifications; Thioethers

Indexed keywords

CARBOHYDRATES; COMPLEXATION; DESULFURIZATION; EXCITONS; GLYCOPROTEINS; PHOSPHORUS COMPOUNDS;

DISULFIDES; GLYCOSYLATION; PROTEIN MODIFICATIONS; THIOETHERS;

PROTEINS;

AMINO ACID; CROSS LINKING REAGENT; DISULFIDE; GLYCOPROTEIN; SULFIDE; THIOL DERIVATIVE;

ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; ELECTROSPRAY MASS SPECTROMETRY;

AMINO ACIDS; CROSS-LINKING REAGENTS; DISULFIDES; GLYCOPROTEINS; MODELS, MOLECULAR; MOLECULAR STRUCTURE; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION; SULFHYDRYL COMPOUNDS; SULFIDES;

EID: 41049108991     PISSN: 14337851     EISSN: None     Source Type: Journal    
DOI: 10.1002/anie.200704381     Document Type: Article

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33. β.
34. Similar yields were observed with hexaethylphosphorus triamide; however, the purification of the product was more cumbersome than when HMPTwas used.
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39. Modification at C156 was corroborated by trypsin digestion and MALDI MS analysis (see the Supporting Information).