Further characterization of the binding of heparin to granulocyte colony-stimulating factor: importance of sulfate groups.
Heparin mediates fundamental biological mechanisms through interaction with proteins. Previously, we have shown that standard heparin binds to granulocyte colony-stimulating factor (G-CSF) with an affinity of 4.8 x 10(5) M(-1). To further study the structural features in heparin that are responsible for this interaction, we studied the bindings of G-CSF and N-desulfated and 2,3-O-desulfated heparin by CZE. Results showed that the N-desulfated heparin had a similar affinity for G-CSF ((5.4 +/- 0.9) x 10(5) M(-1)), but the 2,3-O-desulfated heparin had a 1000-fold lower affinity ((3.4 +/- 1.2) x 10(2) M(-1)) in comparison to standard heparin. The results showed that 2,3-O-sulfate groups are more important than N-sulfate groups in heparin-G-CSF interaction.
Liang
Aiye
A
Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian, China.
Liu
Xiaojun
X
Du
Yuguang
Y
Wang
Keyi
K
Lin
Bingcheng
B
D019075:Electrophoresis, Capillary; D016179:Granulocyte Colony-Stimulating Factor / Q000737:chemistry*; D006493:Heparin / Q000031:analogs & derivatives / Q000737:chemistry*; D006801:Humans; D011485:Protein Binding; D013463:Sulfuric Acid Esters / Q000737:chemistry*
D013463:Sulfuric Acid Esters; C044153:heparin, N-desulfated; C410523:heparin, O-desulfated; D016179:Granulocyte Colony-Stimulating Factor; D006493:Heparin