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Interaction during fibril formation of soluble collagen with cartilage proteinpolysaccharide
Author(s) -
Disalvo Joseph,
Schubert Maxwell
Publication year - 1966
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.1966.360040302
Subject(s) - chemistry , pellet , chondroitin sulfate , centrifugation , precipitation , pellets , ionic strength , fibril , uronic acid , chromatography , cartilage , glycosaminoglycan , matrix (chemical analysis) , polysaccharide , biophysics , biochemistry , organic chemistry , anatomy , aqueous solution , medicine , materials science , physics , oceanography , biology , meteorology , composite material , geology
Precipitation of soluble forms of collagen from solutions containing the soluble protein‐polysaccharide (PP‐L) of bovine nasal cartilage, followed by centrifugation at 100,000 g , resulted in the formation of coherent elastic pellets whose wet weights increased with the concentration of PP‐L in the initial solution. Dry weights and uronic acid contents of these pellets showed that the amount of water held in the wet pellet was nearly constant for any one kind and concentration of collagen, and ranged from 20 to 100 mg./mg. PP‐L in the pellet. Soluble collagens from four different sources and PP‐L from three kinds of cartilage showed similar effects. Precipitation of soluble collagen in the presence of hyaluronate or dextran yielded pellets of much smaller size than those formed in the presence of PP‐L. The presence of chondroitin sulfate had only a slight effect on wet pellet weights. Wet weights of pellets formed in the presence of PP‐L decreased with increasing ionic strength. A model involving entanglement between insoluble collagen fibrils and the relatively stiff chondroitin sulfate chains of branched PP‐L seems qualitatively capable of accounting for these results.