American Society of Hematology

Fig. 5.

$Fig. 5. Confirmation of the size of HS required for optimum binding to MIP1α. / 3H-labeled HS chains were digested with platelet heparinase under different pH conditions, as described in “Materials and methods.” Resultant HS fragments were size fractionated on a Cl-6B Sepharose gel filtration column. (A) Pooled platelet heparinase fractions of average sizes 14 kDa (▴), 10 kDa (●), and 5 kDa (▪) were separately rerun on the Cl-6B Sepharose column to verify their size distribution. Intact (B), 14 kDa (C), 10 kDa (D), and 5 kDa (E) HS fragments were applied to an MIP1α (BB10010) (▪) and to a control Affi-Gel column (●) in 0.15 M NaCl and were eluted with a stepwise NaCl gradient (. . . . . . .). Graphs are representative of 2 experiments.$

Confirmation of the size of HS required for optimum binding to MIP1α.

³H-labeled HS chains were digested with platelet heparinase under different pH conditions, as described in “Materials and methods.” Resultant HS fragments were size fractionated on a Cl-6B Sepharose gel filtration column. (A) Pooled platelet heparinase fractions of average sizes 14 kDa (▴), 10 kDa (●), and 5 kDa (▪) were separately rerun on the Cl-6B Sepharose column to verify their size distribution. Intact (B), 14 kDa (C), 10 kDa (D), and 5 kDa (E) HS fragments were applied to an MIP1α (BB10010) (▪) and to a control Affi-Gel column (●) in 0.15 M NaCl and were eluted with a stepwise NaCl gradient (^{. . . . . . .}). Graphs are representative of 2 experiments.

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