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
Author:
Affiliation:
1. Am Waldplatz 15, D-33098 Paderborn, Germany, and Institute of Medical Physics and Biophysics, University of Münster, Robert-Koch-Str. 31, D-48149 Münster, Germany
Publisher
American Chemical Society (ACS)
Subject
General Chemistry,Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/pr070318r
Reference41 articles.
1. Covalent Crosslinking between Molecules of Type I and Type III Collagen. The Involvement of the N-Terminal, Nonhelical Regions of the alphal(I) and al(III) Chains in the Formation of Intermolecular Crosslinks
2. Structural Characteristics of Cross-Linking Sites in type V Collagen of Bone. Chain Specificities and Heterotypic Links to Type I Collagen
3. Acid Soluble Calf Skin Collagen. Characterization of the Peptides Obtained by Cyanogen Bromide Cleavage of its alphal-Chain
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