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. keygen.hdd.regenerator.2011.CRACKED.Full.211 partituras romero su.Visualization of intermolecular interactions between non-gel forming proteins and polyanionic DNA using transferrin/DNA complex as model.
We have used the transferrin/DNA complex as model of non-gel forming proteins to study the interaction of proteins with anionic biomolecules. The complex is formed by covalent binding of transferrin (Tf) with a defined quantity of DNA (D) using the cyanogen bromide (CNBr) derivative of Tf [Cao et al. J. Biol. Chem. (1981) 256, 7281]. Electron microscopy was used to demonstrate that the Tf-DNA complexes formed by the above modification had a rod-like structure or a regular disc. The interaction between the protein and the DNA was mainly electrostatic. The binding of the transferrin/DNA complex to DNA was analyzed with ethidium bromide (EtBr), and their binding to various materials were examined. The results showed that the binding of the Tf-DNA complex to the serum proteins with negatively charged groups was electrostatic.Q:
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