论文信息 - The structure of pyridinoline, a collagen crosslink.

The structure of pyridinoline, a collagen crosslink.

Abstract Pyridinoline is an amino acid isolated from collagen and probably serves as a crosslink in collagen fiber. This compound was isolated on a large scale from bovine bone and investigated by 1 H-nmr and 13 C-nmr spectroscopy, mass spectroscopy and chemical degradation. The structure is proposed on the basis of these data.

[1] D Fujimoto,et al. Isolation and characterization of a fluorescent material in bovine achilles tendon collagen , 1977 .

[2] W. Korytnyk,et al. [79] Nuclear magnetic resonance spectroscopy of vitamin B6 , 1970 .

[3] M. Glimcher,et al. Analysis of a crosslinked peptide from calf bone collagen: evidence that hydroxylysyl glycoside participates in the crosslink. , 1973, Biochemical and biophysical research communications.

[4] Olga O. Blumenfeld,et al. Structure and Metabolism of Connective Tissue Proteins , 1972 .

[5] P. Gallop,et al. Collagen crosslinking: isolation of hydroxyaldol-histidine, a naturally-occurring crosslink. , 1975, Biochemical and biophysical research communications.

[6] L. Fowler,et al. Chemistry of the collagen cross-links. Isolation and characterization of two intermediate intermolecular cross-links in collagen. , 1970, The Biochemical journal.

[7] A. Katritzky,et al. Degradation Products from Elastin: Proton Magnetic Resonance Spectra of Degradation Products from Elastin , 1963, Nature.