Cyanogen bromide peptides of the fibrillar collagens I, III, and V and their mass spectrometric characterization: Detection of linear peptides, peptide glycosylation, and cross-linking peptides involved in formation of homo- and heterotypic fibrils

Journal of Proteome Research

Volumn 6, Issue 11, 2007, Pages 4269-4289

  Henkel, Werner ^a   Dreisewerd, Klaus ^b  

^a University of Münster ^*  (Germany)

^b UNIVERSITY OF MÜNSTER   (Germany)

Author keywords

Collagens; Cross linking; Cyanogen bromide cleavage; Glycosylation; MALDI MS

Indexed keywords

COLLAGEN TYPE 1; COLLAGEN TYPE 3; COLLAGEN TYPE 5; CYANOGEN BROMIDE; PEPSIN A; PEPTIDE DERIVATIVE;

ALPHA CHAIN; AMINO ACID SEQUENCE; ANIMAL TISSUE; ARTICLE; FETUS; FIBER; MASS SPECTROMETRY; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; NONHUMAN; PRIORITY JOURNAL; PROTEIN CROSS LINKING; PROTEIN GLYCOSYLATION; ULTRAVIOLET RADIATION;

ANIMALS; CATTLE; COLLAGEN; COLLAGEN TYPE I; COLLAGEN TYPE III; COLLAGEN TYPE V; CROSS-LINKING REAGENTS; CYANOGEN BROMIDE; GLYCOSYLATION; MASS SPECTROMETRY; MOLECULAR WEIGHT; PEPTIDES; PROTEIN STRUCTURE, TERTIARY; PROTEINS; PROTEOMICS; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; ULTRAVIOLET RAYS;

BOVINAE;

EID: 36348963174     PISSN: 15353893     EISSN: None     Source Type: Journal    
DOI: 10.1021/pr070318r     Document Type: Article

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