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Effects of glycosaminoglycans and proteoglycan on the in vitro assembly and thermal stability of collagen fibrils
Author(s) -
Snowden John McK.,
Swann David A.
Publication year - 1980
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1980.360190405
Subject(s) - chemistry , fibril , proteoglycan , glycosaminoglycan , kinetics , dermatan sulfate , biophysics , chondroitin sulfate , in vitro , thermal stability , ionic strength , decorin , biochemistry , hyaluronic acid , extracellular matrix , organic chemistry , aqueous solution , anatomy , physics , quantum mechanics , biology , medicine
The effects of three glycosaminoglycans (chondroitin 6‐sulfate, dermatan sulfate, and hyaluronate) and a proteoglycan on the kinetics of fibril formation and on the thermal stability of the in vitro assembled collagen fibrils, under physiological conditions of ionic strength and pH, have been examined. The glycosaminoglycans were found to influence the kinetics of collagen precipitation but not the thermal stability of the in vitro assembled fibrils. The proteoglycan was found to influence the kinetics of collagen precipitation and to reduce the thermal stability of the in vitro assembled fibrils. Comparison of the interaction occurring between chondroitin 6‐sulfate and collagen under acidic conditions (0.05 M acetic acid) and that occurring under physiological conditions showed that markedly different interaction products were formed under the different conditions.