TY - JOUR
T1 - High-performance gel permeation chromatography of glycosaminoglycans column calibration by gel electrophoresis
AU - Hittner, Daniel M.
AU - Cowman, Mary K.
N1 - Funding Information:
The authors wish to thank Mr . H . Min and Mr . H . G . Lee for their kind technical assistance . This research was supported by NIH Grant EY 04804. A preliminary account of this work was presented at the 13th International Carbohydrate Symposium, Ithaca, NY, August 10-15,1986 .
PY - 1987
Y1 - 1987
N2 - High-performance gel permeation chromatography and sensitivity-enhanced polyacrylamide gel electrophoresis (SE-PAGE) have been combined to investigate the chromatographic properties of structurally related glycosaminoglycans. Enzymatically digested samples of hyaluronate, chondroitin 4-sulfate and dermatan sulfate were fractionated on a column series of TSK G4000SW and TSK G2000SW, eluted with 0.15 M sodium chloride. Isolated fractions were subjected to sensitivity-enhanced polyacrylamide gel eletrophoresis for determination of molecular weight. These procedures allowed the rapid development of column calibration profiles for each glycosaminoglycan, under a given set of chromatographic conditions. The profiles obtained in 0.15 M sodium chloride yielded the following data: (1) at equal degrees of polymerization, hyaluronic acid chains have an apparently smaller hydrodynamic radius than the sulfated polymers, and (2) at equal molecular weights, all three glycosaminoglycans have approximately equal hydrodynamic radii.
AB - High-performance gel permeation chromatography and sensitivity-enhanced polyacrylamide gel electrophoresis (SE-PAGE) have been combined to investigate the chromatographic properties of structurally related glycosaminoglycans. Enzymatically digested samples of hyaluronate, chondroitin 4-sulfate and dermatan sulfate were fractionated on a column series of TSK G4000SW and TSK G2000SW, eluted with 0.15 M sodium chloride. Isolated fractions were subjected to sensitivity-enhanced polyacrylamide gel eletrophoresis for determination of molecular weight. These procedures allowed the rapid development of column calibration profiles for each glycosaminoglycan, under a given set of chromatographic conditions. The profiles obtained in 0.15 M sodium chloride yielded the following data: (1) at equal degrees of polymerization, hyaluronic acid chains have an apparently smaller hydrodynamic radius than the sulfated polymers, and (2) at equal molecular weights, all three glycosaminoglycans have approximately equal hydrodynamic radii.
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U2 - 10.1016/0021-9673(87)80013-4
DO - 10.1016/0021-9673(87)80013-4
M3 - Article
C2 - 3654861
AN - SCOPUS:0023669252
SN - 0021-9673
VL - 402
SP - 149
EP - 158
JO - Journal of Chromatography A
JF - Journal of Chromatography A
IS - C
ER -