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. 1981 Jun 15;196(3):693–698. doi: 10.1042/bj1960693

Fluorimetric study of the binding of protoporphyrin to haemopexin and albumin.

A A Lamola, I Asher, U Muller-Eberhard, M Poh-Fitzpatrick
PMCID: PMC1163087  PMID: 7317009

Abstract

Fluorescence spectra of protoporphyrin bound to its most affinitive site on human serum albumin, bound to human haemopexin and dissolved in human plasma reveal that, when present in plasma, at least 90% of this porphyrin is bound to albumin. Human serum albumin binds protoporphyrin with an affinity KA = 3 X 10(9)M-1 in phosphate-buffered saline. The affinity of haemopexin for protoporphyrin is 4 times smaller. From these data it is concluded that less than 1% of plasma protoporphyrin is bound to haemopexin. Implications of the data for protoporphyrin transport and clearance are discussed.

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Selected References

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