Skip to main content
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1968 Oct;61(2):708–716. doi: 10.1073/pnas.61.2.708

The cross-linking of collagen and elastin: enzymatic conversion of lysine in peptide linkage to alpha-aminoadipic-delta-semialdehyde (allysine) by an extract from bone.

S R Pinnell, G R Martin
PMCID: PMC225217  PMID: 5246001

Full text

PDF
708

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bird D. W., Savage J. E., O'Dell B. L. Effect of copper deficiency and inhibitors on the amine oxidase activity of chick tissues. Proc Soc Exp Biol Med. 1966 Oct;123(1):250–254. doi: 10.3181/00379727-123-31458. [DOI] [PubMed] [Google Scholar]
  2. Bornstein P., Kang A. H., Piez K. A. The nature and location of intramolecular cross-links in collagen. Proc Natl Acad Sci U S A. 1966 Feb;55(2):417–424. doi: 10.1073/pnas.55.2.417. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bornstein P., Piez K. A. The nature of the intramolecular cross-links in collagen. The separation and characterization of peptides from the cross-link region of rat skin collagen. Biochemistry. 1966 Nov;5(11):3460–3473. doi: 10.1021/bi00875a012. [DOI] [PubMed] [Google Scholar]
  4. Higashino K., Fujioka M., Aoki T., Yamamura T. Metabolism of lysine in rat liver. Biochem Biophys Res Commun. 1967 Oct 11;29(1):95–100. doi: 10.1016/0006-291x(67)90547-5. [DOI] [PubMed] [Google Scholar]
  5. Hill C. H., Starcher B., Kim C. Role of copper in the formation of elastin. Fed Proc. 1967 Jan-Feb;26(1):129–133. [PubMed] [Google Scholar]
  6. LEVENE C. I., GROSS J. Alterations in state of molecular aggregation of collagen induced in chick embryos by beta-aminopropionitrile (lathyrus factor). J Exp Med. 1959 Nov 1;110:771–790. doi: 10.1084/jem.110.5.771. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Miller E. J., Martin G. R., Mecca C. E., Piez K. A. The biosynthesis of elastin cross-links. The effect of copper deficiency and a lathyrogen. J Biol Chem. 1965 Sep;240(9):3623–3627. [PubMed] [Google Scholar]
  8. Miller E. J., Piez K. A. An accelerated single-column procedure for the automatic analysis of amino acids in collagen and elastin hydrolyzates. Anal Biochem. 1966 Aug;16(2):320–326. doi: 10.1016/0003-2697(66)90161-8. [DOI] [PubMed] [Google Scholar]
  9. Miller E. J., Pinnell S. R., Martin G. R., Schiffmann E. Investigation of the nature of the intermediates involved in desmosine biosynthesis. Biochem Biophys Res Commun. 1967 Jan 23;26(2):132–137. doi: 10.1016/0006-291x(67)90224-0. [DOI] [PubMed] [Google Scholar]
  10. PIEZ K. A. Continuous scintillation counting of carbon-14 and tritium in effluent of the automatic amino acid analyzer. Anal Biochem. 1962 Dec;4:444–458. doi: 10.1016/0003-2697(62)90126-4. [DOI] [PubMed] [Google Scholar]
  11. Page R. C., Benditt E. P. Interaction of the lathyrogen beta-aminopropionitrile (BAPN) with a copper-containing amine oxidase. Proc Soc Exp Biol Med. 1967 Feb;124(2):454–459. doi: 10.3181/00379727-124-31763. [DOI] [PubMed] [Google Scholar]
  12. Page R. C., Benditt E. P. Molecular diseases of connective and vascular tissues. II. Amine oxidase inhibition by the lathyrogen, beta-aminopropionitrile. Biochemistry. 1967 Apr;6(4):1142–1148. doi: 10.1021/bi00856a025. [DOI] [PubMed] [Google Scholar]
  13. Partridge S. M. Biosynthesis and nature of elastin structures. Fed Proc. 1966 May-Jun;25(3):1023–1029. [PubMed] [Google Scholar]
  14. Pinnell S. R., Martin G. R., Miller E. J. Desmosine biosynthesis: nature of inhibition by D-penicillamine. Science. 1968 Aug 2;161(3840):475–476. doi: 10.1126/science.161.3840.475. [DOI] [PubMed] [Google Scholar]
  15. Popenoe E. A., Aronson R. B., Van Slyke D. D. Hydroxylysine formation from lysine during collagen biosynthesis. Proc Natl Acad Sci U S A. 1966 Feb;55(2):393–397. doi: 10.1073/pnas.55.2.393. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES