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 } 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.
Dates
Type | When |
---|---|
Created | 10 years ago (Aug. 10, 2015, 4:28 p.m.) |
Deposited | 3 years, 9 months ago (Nov. 25, 2021, 10:39 a.m.) |
Indexed | 1 year, 8 months ago (Jan. 2, 2024, 12:09 p.m.) |
Issued | 44 years, 2 months ago (June 15, 1981) |
Published | 44 years, 2 months ago (June 15, 1981) |
Published Print | 44 years, 2 months ago (June 15, 1981) |
@article{Lamola_1981, title={Fluorimetric study of the binding of protoporphyrin to haemopexin and albumin}, volume={196}, ISSN={0264-6021}, url={http://dx.doi.org/10.1042/bj1960693}, DOI={10.1042/bj1960693}, number={3}, journal={Biochemical Journal}, publisher={Portland Press Ltd.}, author={Lamola, A A and Asher, I and Muller-Eberhard, U and Poh-Fitzpatrick, M}, year={1981}, month=jun, pages={693–698} }