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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Increased heparin binding by site directed mutagenesis of a recombinant chimera of bombyxin and insulin-like growth factor II.

BOMIGF, a chimera between bombyxin and insulin-like growth factor II (IGF II) has been modified and extended to a total of 85 amino acids including 7 additional basic amino acids. The new peptide bound heparin as efficiently as GM-CSF and much better than IGF II or BOMIGF. It could be retained on albumin-coated tissue culture wells without loosing its capacity to stimulate thymidine incorporation into erythroid cells of fetal bovine liver and on fibronectin-heparin coated wells keeping its mitogenic activity towards L6 muscle cells.[1]

References

  1. Increased heparin binding by site directed mutagenesis of a recombinant chimera of bombyxin and insulin-like growth factor II. Congote, L.F. Biochim. Biophys. Acta (1995) [Pubmed]
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