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Heparin-binding properties of lactoferrin and lysozyme.

Comparative biochemistry and physiology. B, Comparative biochemistry (1992-12-01)
S Zou, C E Magura, W L Hurley
ABSTRACT

1. Binding of biotin-heparin to immobilized lactoferrin and lysozyme was optimum at pH 6.0, 100 mM NaCl. Complex interactions between NaCl and CaCl2 concentrations were observed for heparin binding to both proteins. 2. The metal ions Cu2+, Zn2+, Fe2+ and Fe3+ inhibited heparin binding, with half-maximal inhibition of binding to lactoferrin occurring between 600 microM and 1 mM and for lysozyme between 500 and 800 microM. 3. Binding of biotin-heparin to both proteins was inhibited to varying degrees by heparin, heparan sulfate, chondroitin sulfate A, dextran sulfate and DNA.

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Sigma-Aldrich
Heparin−biotin sodium salt, ≥97%