Impact of K 2 PtCl 4 on the structure of human serum albumin and its binding ability of heme and bilirubin
Journal of Inorganic Biochemistry, ISSN: 0162-0134, Vol: 53, Issue: 4, Page: 249-260
1994
- 12Citations
- 5Captures
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Article Description
Absorption, CD, gel-filtration chromatography, and immunological tests were used to evaluate the interactions of K 2 PtCl 4 with human serum albumin. Multidentate coordination of Pt(II) to HSA causes distinct variations in the protein conformation including a considerable decrease of the helical structure. The high excess of Pt(II) ions leads to dimerization of the protein. The metal ion binding weakens the interactions of HSA with other molecules like heme or bilirubin.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/0162013494851123; http://dx.doi.org/10.1016/0162-0134(94)85112-3; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0028176601&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/8169606; https://linkinghub.elsevier.com/retrieve/pii/0162013494851123; http://dx.doi.org/10.1016/0162-0134%2894%2985112-3; https://dx.doi.org/10.1016/0162-0134%2894%2985112-3
Elsevier BV
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