We reported',\* that Sepharose CL-4B gel can retain sulfated glycosaminoglycuronans in concentrated ammonium sulfate solution at low temperature, resulting in an unique separation of the molecular species by stepwise elution of decreasing concentration of ammonium sulfate. The fractionation of shark
A study on heterogeneity in molecular species of shark cartilage chondroitin sulfate C. Fractionation of the polysaccharide on sepharose CL-4B in the presence of high concentrations of ammonium sulfate
โ Scribed by Akira Ogamo; Toshiharu Yamada; Kinzo Nagasawa
- Publisher
- Elsevier Science
- Year
- 1987
- Tongue
- English
- Weight
- 550 KB
- Volume
- 165
- Category
- Article
- ISSN
- 0008-6215
No coin nor oath required. For personal study only.
โฆ Synopsis
Shark cartilage chondroitin sulfate C was fractionated by chromatography on Sepharose CL-4B-2.5 to 1.5M ammonium sulfate in 10mM hydrochloric acid at 4 degrees. Both unit-disaccharide composition and molecular-size distribution clearly affected the fractionation. Comparison of this fractionation with the fractionation on Sepharose 6B gel in 0.2M sodium chloride revealed that the former is distinctly superior to the latter. The fractionation on Sepharose CL-4B in the presence of ammonium sulfate also showed that the chondroitin sulfate C molecules having a larger molecular size contain generally more chondroitin 6-sulfate units (as major constituent) and less chondroitin disulfate units (D type, as minor constituent) than those having a smaller molecular size).
๐ SIMILAR VOLUMES
The effect of bound sulfate groups and uronic acid residues of glycosaminoglycans on their behavior in chromatography on hydrophobic gel was examined by the use of several pairs of depolymerized chondroitin, chondroitin 4- or 6-sulfate, and dermatan sulfate having comparable degree of polymerization