Journal of Biological Chemistry · 1968 · 33 citations · 17 references
Life SciencesBiochemistryProtein BiochemistryProteomicsSequence AnalysisConnective TissueCuticle StructureFibrous ProteinsGlycan StructurePeptide AnalysisProteolytic EnzymesCollagen BiologyHydroxyproline ContentLarval Cuticle StructureMolecular Architecture Of CollagenSynthetic Peptide Characterization
Abstract Salt-soluble collagen of earthworm cuticle contains much hydroxyproline in the second position of tripeptide sequences beginning with glycine, as determined by sequence analysis of mixed peptides released by the action of clostridial collagenase. A tripeptide, Gly-Hyp-Ala, was isolated from these digests and identified by sequence analysis and by comparison with a synthetic reference peptide. It was estimated to account for approximately 10% of the hydroxyproline of both purified salt-soluble collagen and of the total collagen of the cuticle.
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The Structure of Human Hemoglobin
William H. Konigsberg, Robert Hill · Journal of Biological Chemistry · 1962 · 316 citations · Full text