Fig. 6.
Fig. 6. Affinity of unmodified and O-sulfated heparins for thrombospondin. / The affinity of unmodified or O-sulfated heparin for TSP was examined using affinity coelectrophoresis. 125I-labeled GAGs were electrophoresed through varying concentrations of TSP (0 to 100 nM). Half-maximal binding (EC50; a measure of affinity) was calculated as the concentration of TSP (in nM) at which retardation of migration of the GAGs (R; a function of binding) was 50%.

Affinity of unmodified and O-sulfated heparins for thrombospondin.

The affinity of unmodified or O-sulfated heparin for TSP was examined using affinity coelectrophoresis. 125I-labeled GAGs were electrophoresed through varying concentrations of TSP (0 to 100 nM). Half-maximal binding (EC50; a measure of affinity) was calculated as the concentration of TSP (in nM) at which retardation of migration of the GAGs (R; a function of binding) was 50%.

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