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

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Comparative studies of pregnancy associated plasma protein-A and alpha 2-macroglobulin using metal chelate chromatography.

Pregnancy Associated Plasma Protein-A (PAPP-A), shares many physicochemical and functional similarities with alpha-2-macroglobulin (alpha 2M). Comparative studies between these two proteins and various metal chelate Sepharoses have shown that both PAPP-A and alpha 2M bind to the copper and zinc, but not to the calcium, manganese or magnesium chelate gels. In addition to PAPP-A and alpha 2M, fibronectin and Pregnancy Zone Protein (PZP) were also found to bind to the copper and zinc chelate gels. Analysis of proteins bound to the zinc chelate Sepharose showed alpha 2M to have the highest affinity for the matrix, followed by PAPP-A and fibronectin, which coeluted, and then PZP. Following the zinc chelate chromatography minor qualitative changes were detected only in PAPP-A, but the eluted proteins retained in-vitro functional activity. By atomic absorption, PAPP-A, alpha 2M and fibronectin were found to contain zinc.[1]

References

  1. Comparative studies of pregnancy associated plasma protein-A and alpha 2-macroglobulin using metal chelate chromatography. Sinosich, M.J., Davey, M.W., Teisner, B., Grudzinskas, J.G. Biochem. Int. (1983) [Pubmed]
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