[High-resolution 13C-NMR spectra of collagen peptides].
Relative intensities of main resonance high-resolution 13C NMR spectra of acid hydrolysis products of bovine skin and human aortic collagens were measured. The contents of Gly, Pro, Hyp amino acid residues and Gly-Pro-Y triplets in collagen peptides was estimated. A good agreement between the experimental and theoretical data of the analysis of amino acid sequences of bovine skin collagen was shown.
D000595:Amino Acid Sequence; D000818:Animals; D001011:Aorta / Q000032:analysis; D002417:Cattle; D003094:Collagen / Q000032:analysis*; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D010455:Peptides / Q000032:analysis*; D012867:Skin / Q000032:analysis
D010455:Peptides; D003094:Collagen
Spektry 13C-IaMR vysokogo razresheniia peptidov kollagena.