ArticleThe Journal of biological chemistry2010
Metal ions and electrolytes regulate the dissociation of heme from human hemopexin at physiological pH.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
2 citing papers in PubMed, 5 citations in OpenAlex.
- Article
- An alternative view of the proposed alternative activities of hemopexin.Protein science : a publication of the Protein Society · 2011Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The stability of the hemopexin-heme (Hx-heme) complex to dissociation of the heme prosthetic group has been examined in bicarbonate buffers in the presence and absence of various divalent metal ions. In NH(4)HCO(3) buffer (pH 7.4, 20 mm, 25 degrees C) containing Zn(2+) (100 microm), 14% of the heme dissociates from this complex (4.5 microm) within 10 min, and 50% dissociates within 2 h. In the absence of metal ions, the rate of dissociation of this complex is far lower, is decreased further in KHCO(3) solution, and is minimal in NaHCO(3). In NH(4)HCO(3) buffer, dissociation of the Hx-heme complex is accelerated by addition of divalent metals with decreasing efficiency in the order Zn(2+) > Cu(2+) >> Ni(2+) > Co(2+)>>Mn(2+). Addition of Ca(2+) prior to addition of Zn(2+) stabilizes the Hx-heme complex to dissociation of the heme group, and addition of Ca(2+) after Zn(2+)-induced dissociation of the Hx-heme complex results in re-formation of the Hx-heme complex. These effects are greatly accelerated at 37 degrees C and diminished in other buffers. Overall, the solution conditions that promote formation of the Hx-heme complex are similar to those found in blood plasma, and conditions that promote release of heme are similar to those that the Hx-heme complex should encounter in endosomes following endocytosis of the complex formed with its hepatic receptor.
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Registered trials
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