Analysis of cyanogen bromide peptides of type I collagen from a patient with lethal osteogenesis imperfecta.

Abstract

The CNBr peptides of type I collagen from bone of a patient with lethal osteogenesis imperfecta and age-matched controls were isolated by molecular-sieve chromatography and their amino acid compositions were determined. No differences were found between the compositions of the peptides from the patient and those from the controls, except for an increase in the degree of hydroxylation of lysine in all peptides from the patient. Type I collagen CNBr peptides from chick-embryo skin [Barnes, Constable Morton & Kodicek (1971) Biochem. J. 125, 925--928] and guinea-pig scar tissue [Shuttleworth, Forrest & Jackson (1975) Biochim. Biophys. Acta 379, 207--216] also have an increased degree of hydroxylation of lysine with an otherwise normal amino acid composition, and it was believed that this could be an embryonic form of collagen. As a similar collagen was present in the bones of the patient studied, it seems possible that the same 'embryonic' collagen is synthesized during development, in repair process and also in genetic disorders of collagen metabolism.

• Authors: E Kirsch, R W Glanville, T Krieg, P Müller
• Journal: The Biochemical journal (Biochem J) Vol. 211 Issue 3 Pg. 599-603 (Jun 01 1983) ISSN: 0264-6021 [Print] England
• PMID: 6411063 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Amino Acids
• Peptide Fragments
• Hydroxylysine
• Collagen
• Lysine
• Cyanogen Bromide

Topics

• Amino Acids (analysis)
• Chemical Phenomena
• Chemistry
• Chromatography, Gel
• Collagen (metabolism)
• Cyanogen Bromide
• Electrophoresis, Polyacrylamide Gel
• Humans
• Hydroxylysine (analysis)
• Infant
• Lysine (analysis)
• Osteogenesis Imperfecta (metabolism)
• Peptide Fragments