Evidence for the chemical modification of collagen in rheumatoid arthritis.
Open Access
- 1 September 1965
- journal article
- research article
- Published by Elsevier in Annals of the Rheumatic Diseases
- Vol. 24 (5) , 473-476
- https://doi.org/10.1136/ard.24.5.473
Abstract
All the rheumatoid collagen shows an increase in gelatin formation with time of pronase digestion in contrast to the normal collagen which does not change. The primary structure of collagen derived from rheumatoid tissue is different from normal collagen. This difference may be either a cause or a result of the disease or may even be the result of general inflammation of the disease tissue. The collagen is chemically modified in rheumatoid tissues. Peptide bonds cleaved by pronase in rheumatoid collagens should be examined.This publication has 4 references indexed in Scilit:
- Nishihara Technique for the Solubilization of CollagenAnnals of the Rheumatic Diseases, 1964
- Tropocollagen: Significance of Protease-Induced AlterationsScience, 1963
- An enzyme system in the gastric secretion capable of reducing the viscosity of native soluble calf-skin collagenBiochimica et Biophysica Acta, 1963
- THE EFFECTS OF PROTEASES ON THE TROPOCOLLAGEN MACROMOLECULE AND ON ITS AGGREGATION PROPERTIESProceedings of the National Academy of Sciences, 1960