Haem peptide–protein interactions. Part 2. — Kinetics and mechanism of the interaction of microperoxides-8 with apomyoglobin
Author:
Publisher
Royal Society of Chemistry (RSC)
Subject
General Chemistry
Link
http://pubs.rsc.org/en/content/articlepdf/1989/F1/F19898503845
Cited by 5 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Properties and Reactivity of Myoglobin Reconstituted with Chemically Modified Protohemin Complexes;Biochemistry;2000-07-08
2. Monomeric ferric heme peptide derivatives: Model systems for hemoproteins;Journal of Inorganic Biochemistry;1995-12
3. Haem peptide/protein interaction part 6: The kinetic mechanisms of the interactions with, and inhibition of enzymic activity of the human erythrocyte glutathione S-transferase isoenzyme rho (p), by haem octa-, nona-, and undecapeptides MP-8/-9/-11;Journal of Inorganic Biochemistry;1994-02
4. Haem-peptide-protein interactions: Part 5. The haem undecapeptide microperoxidase-11 (Fe3+MP-11)/human serum albumin (HSA) reaction in aqueous methanolic solution. A simple system demonstrating the effect of hydrophobicity on ligand release from a ligand-protein complex;Journal of Inorganic Biochemistry;1993-04
5. Haem peptide–protein interactions. Part 3.—The kinetics and mechanism of the interaction between human placental glutathione S-transferase π and the non-substrate ligand microperoxidase-8 (MP-8);J. Chem. Soc., Faraday Trans.;1990
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