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A novel methodology for assignment of disulfide bond pairings in proteins.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Wu, J. Watson, J. T.
Description	Country affiliation: United States Author Affiliation: Wu J ( Department of Chemistry, Michigan State University, East Lansing 48824, USA.)
Abstract	A novel methodology is described for the assignment of disulfide bonds in proteins of known sequence. The denatured protein is subjected to limited reduction by tris(2-carboxyethyl)phosphine (TCEP) in pH 3.0 citrate buffer to produce a mixture of partially reduced protein isomers; the nascent sulfhydryls are immediately cyanylated by 1-cyano-4-dimethylamino-pyridinium tetrafluoroborate (CDAP) under the same buffered conditions. The cyanylated protein isomers, separated by and collected from reversed-phase HPLC, are subjected to cleavage of the peptide bonds on the N-terminal side of cyanylated cysteines in aqueous ammonia to form truncated peptides that are still linked by residual disulfide bonds. The remaining disulfide bonds are then completely reduced to give a mixture of peptides that can be mass mapped by MALDI-MS. The masses of the resulting peptide fragments are related to the location of the paired cysteines that had undergone reduction, cyanylation, and cleavage. A side reaction, beta-elimination, often accompanies cleavage and produces overlapped peptides that provide complementary confirmation for the assignment. This strategy minimizes disulfide bond scrambling and is simple, fast, and sensitive. The feasibility of the new approach is demonstrated in the analysis of model proteins that contain various disulfide bond linkages, including adjacent cysteines. Experimental conditions are optimized for protein partial reduction, sulfhydryl cyanylation, and chemical cleavage reactions.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	2
Volume Number	6
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	1997-02-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Disulfides Chemistry Proteins Chromatography, High Pressure Liquid Indicators And Reagents Isomerism Peptide Fragments Peptide Mapping Phosphines Spectrometry, Mass, Matrix-assisted Laser Desorption-ionization Sulfhydryl Compounds Research Support, Non-u.s. Gov't Research Support, U.s. Gov't, P.h.s. Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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