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Further characterization of the binding of heparin to granulocyte colony‐stimulating factor: Importance of sulfate groups
Author(s) -
Liang Aiye,
Liu Xiaojun,
Du Yuguang,
Wang Keyi,
Lin Bingcheng
Publication year - 2008
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.200700480
Subject(s) - heparin , chemistry , granulocyte , granulocyte colony stimulating factor , sulfate , heparan sulfate , biochemistry , stereochemistry , biology , immunology , organic chemistry , genetics , chemotherapy
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 4.8×10 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)×10 5 M −1 ), but the 2,3‐ O ‐desulfated heparin had a 1000‐fold lower affinity ((3.4 ± 1.2)×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.