Characterization of cysteine residues and disulfide bonds in proteins by liquid chromatography/electrospray ionization tandem mass spectrometry

Cysteine residues and disulfide bonds are important for protein structure and function. We have developed a simple and sensitive method for determining the presence of free cysteine (Cys) residues and disulfide bonded Cys residues in proteins (

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Bibliographic Details
Published in:Journal of mass spectrometry. 2000-08, Vol.35 (8), p.990-1002
Main Authors: Yen, Ten-Yang, Joshi, Rajesh K., Yan, Hui, Seto, Nina O. L., Palcic, Monica M., Macher, Bruce A.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Analytical, structural and metabolic biochemistry
Animals
Biological and medical sciences
biotin
Chromatography, Liquid - methods
cysteine
Cysteine - chemistry
disulfide
Disulfides - chemistry
electrospray
Fundamental and applied biological sciences. Psychology
General aspects, investigation methods
Glycosyltransferases - chemistry
Humans
Hydrogen-Ion Concentration
Lactoglobulins - chemistry
liquid chromatography/tandem mass spectrometry
Mass Spectrometry - methods
N-Acetyllactosamine Synthase - chemistry
Ovalbumin - chemistry
Protein Denaturation
Proteins
Proteins - chemistry
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Description
Summary:Cysteine residues and disulfide bonds are important for protein structure and function. We have developed a simple and sensitive method for determining the presence of free cysteine (Cys) residues and disulfide bonded Cys residues in proteins (
ISSN:1076-5174
1096-9888
DOI:10.1002/1096-9888(200008)35:8<990::AID-JMS27>3.0.CO;2-K