Different levels of glycosylation contribute to the heterogeneity of alpha 1(II) collagen chains derived from a transplantable rat chondrosarcoma.

@article{Furuto1983DifferentLO,
  title={Different levels of glycosylation contribute to the heterogeneity of alpha 1(II) collagen chains derived from a transplantable rat chondrosarcoma.},
  author={D K Furuto and Edward J. Miller},
  journal={Archives of biochemistry and biophysics},
  year={1983},
  volume={226 2},
  pages={604-11}
}
Three collagen fractions, each of which contain molecules composed of alpha 1(II) chains, have been isolated from pepsin-solubilized rat chondrosarcoma collagen. One fraction could be selectively precipitated from the pepsin digest at 0.7 M NaCl. Two additional fractions were obtained on chromatography of the collagen precipitating at 1.2 M NaCl on carboxymethyl cellulose under nondenaturing conditions. When chromatographed on carboxymethyl cellulose under denaturing conditions, each fraction… CONTINUE READING