Characterization of disulfide bond position in proteins and sequence analysis of cystine-bridged peptides by tandem mass spectrometry

Analytical Biochemistry

Volumn 201, Issue 2, 1992, Pages 216-226

  Bean, Mark F ^a   Carr, Steven A ^a  

^a GLAXOSMITHKLINE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

BRIDGED PEPTIDE; CYSTINE; RECOMBINANT DNA; TRANSFORMING GROWTH FACTOR ALPHA;

AMINO ACID SEQUENCE; ARTICLE; DISULFIDE BOND; DNA DETERMINATION; PEPTIDE MAPPING; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN FOLDING; TANDEM MASS SPECTROMETRY;

AMINO ACID SEQUENCE; CYSTINE; DISULFIDES; MOLECULAR SEQUENCE DATA; OXIDATION-REDUCTION; PEPTIDE MAPPING; PEPTIDES; PROTEINS; SPECTRUM ANALYSIS, MASS;

COVALENT BONDS; CYSTINES; IONS; MASS SPECTROMETRY; SULFUR COMPOUNDS;

COLLISIONALLY ACTIVATED DISSOCIATION; PEPTIDE SEQUENCES; PRODUCT ION SPECTRA; PROTEIN SEQUENCES; RELATED PRODUCTS; SEQUENCE ANALYSIS; TANDEM MASS SPECTROMETRY; TRANSFORMING GROWTH FACTORS;

PEPTIDES;

EID: 0026561566     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/0003-2697(92)90331-Z     Document Type: Article

References (23)

1. Peptide studies using a fast atom bombardment high field mass spectrometer and data system. 2—characteristics of positive ionization spectra of peptides,m/z 858 tom/z 5729
2. Fast atom bombardment (FAB) mass spectra of protein digests: Hen and duck egg-white lysozymes
3. Location of disulfide bonds in antithrombin III