Dityrosine in Collagen
- 1 January 1976
- journal article
- research article
- Published by Informa UK Limited in Connective Tissue Research
- Vol. 4 (4), 219-222
- https://doi.org/10.3109/03008207609152224
Abstract
Dityrosine was formed by the action of peracetic acid and sodium peroxide on soluble collagens. Dityrosine was also detected in native insoluble collagen, but only from old animals. Dityrosine was identified by amino acid analysis, fluorescence absorption and mass spectra.This publication has 7 references indexed in Scilit:
- Information contained in the amino acid sequence of theα1(I)-chain of collagen and its consequences upon the formation of the triple helix, of fibrils and crosslinksMolecular and Cellular Biochemistry, 1975
- Stable, nonreducible cross-links of mature collagenBiochemistry, 1975
- Isolation and Characterisation of the Peptides Derived from the α1‐Chain of Calf Skin Collagen after Hydroxylamine CleavageEuropean Journal of Biochemistry, 1970
- Investigation of the products of an enzymic hydrolysis of collagensBiochemistry, 1969
- Formation of insoluble gels and dityrosine by the action of peroxidase on soluble collagensBiochemical and Biophysical Research Communications, 1968
- Evidence for dityrosine in elastinBiochemical and Biophysical Research Communications, 1967
- Characterization of a new type of cross-linkage in resilin, a rubber-like proteinBiochimica et Biophysica Acta, 1963