Increase of Peroxidase Activity of Haptoglobin (2-2)-Hemoglobin at Pathologic Temperature and Presence of Antibiotics
Commenced in January 2007
Frequency: Monthly
Edition: International
Paper Count: 33093
Increase of Peroxidase Activity of Haptoglobin (2-2)-Hemoglobin at Pathologic Temperature and Presence of Antibiotics

Authors: M Tayari, SZ Moosavi-nejad, A Shabani, M Rezaei Tavirani

Abstract:

Free Hemoglobin promotes the accumulation of hydroxyl radicals by the heme iron, which can react with endogenous hydrogen peroxide to produce free radicals which may cause severe oxidative cell damage. Haptoglobin binds to Hemoglobin strongly and Haptoglobin-Hemoglobin binding is irreversible. Peroxidase activity of Haptoglobin(2-2)-Hemoglobin complex was assayed by following increase of absorption of produced tetraguaiacol as the second substrate of Haptoglobin-Hemoglobin complex at 470 nm and 42°C by UV-Vis spectrophotometer. The results have shown that peroxidase activity of Haptoglobin(2-2)-Hemoglobin complex is modulated via homotropic effect of hydrogen peroxide as allostric substrate. On the other hand antioxidant property of Haptoglobin(2- 2)-Hemoglobin was increased via heterotropic effect of the two drugs (especially ampicillin) on peroxidase activity of the complex. Both drugs also have mild effect on quality of homotropic property of peroxidase activity of Haptoglobin(2-2)-Hemoglobin complex. Therefore, in vitro studies show that the two drugs may help Hp-Hb complex to remove hydrogen peroxide from serum at pathologic temperature ature (42 C).

Keywords: Haptoglobin, Hemoglobin, Antioxidant, Antibiotics.

Digital Object Identifier (DOI): doi.org/10.5281/zenodo.1081325

Procedia APA BibTeX Chicago EndNote Harvard JSON MLA RIS XML ISO 690 PDF Downloads 2269

References:


[1] Delanghe J. R. & Langlois M. R. "Haptoglobin polymorphism and body iron stores. Clinical Chemistry and Laboratory Medicine" (2002); 40:212-216.
[2] Sadrzadeh S. M, Graf E, Panter S. S, Hallaway P. E, Eaton J. W. "Hemoglobin a biologic fenton reagent". J Biol Chem (1984). 259:14354-14356.
[3] Cooper C. E, Silaghi-Dumitrescu R, Rukengwa M, Alayash A, Buehler PW. "Peroxidase activity of hemoglobin towards ascorbate and urate: A synergistic protective strategy against toxicity of hemoglobin-based oxygen carriers". Biochimica et Biophysica Acta (2008); 1415-1420.
[4] Langlois MR & Delanghe JR. "Biological and clinical significance of haptoglobin polymorphism in humans". Clinical Chemistry (1996); 42:1589-1600.
[5] Van Vlierberghe H, Langlois M & Delanghe J. "Haptoglobin polymorphisms and iron homeostasis in health and in disease". Clinica Chimica Acta (2004); 345:35-42.
[6] Alfsen A., Waks M. "The hemoglobin binding and activation by haptoglobins: spectrophotometric and potentiometric measurments". biochemical and biophysical research communications (1966); 23:62-67.
[7] Adams E. C. & Weiss MR. "Calorimetric studies of the haemoglobinhaptoglobin reaction". Biochemical Journal (1969); 115:441-447.
[8] Chiancone E, Alfsen A, Ioppolo C, Vecchini P, Agr├▓ AF, Wyman J & Antonini E. "Studies on the reaction of haptoglobin with haemoglobin and haemoglobin chains". I. Stoichiometry and affinity. Journal of Molecular Biology (1968); 34:347-356.
[9] Laurell C. B. "Purification and properties of different haptoglobins". Clinica Chimica Acta (1959); 4:79-81.
[10] Nagel R. L & Gibson QH. "The binding of hemoglobin to haptoglobin and its relation to subunit dissociation of hemoglobin". Journal of Biological Chemistry (1971); 246:69-73.
[11] Peacock A. C. Pastewka JV, Reed RA & Ness AT. "Haptoglobinhemoglobin interaction. Stoichiometry". Biochemistry (1970); 9:2275- 2279.
[12] McCormick D. J. & Atassi MZ. "Hemoglobin binding with haptoglobin: Delineation of the haptoglobin binding site on the ╬▒-chain of human hemoglobin". Journal of Protein Chemistry (1990); 9:735-742.
[13] Theilgaard-Mönch K, Jacobsen LC, Nielsen MJ, Rasmussen T, Udby L, Gharib M, Arkwright PD, Gombart AF, Calafat J, Moestrup SK, Porse BT and Borregaard N. "Haptoglobin is synthesized during granulocytic differentiation, stored in specific granules, and released by neutrophils in response to activation". Blood, in press. (2006).
[14] Connell G. E. & Smithies O. "Human haptoglobins: estimation and purification". The Biochemical journal (1959); 72:115-121.
[15] Melamed-Frank M, Lache O, Enav BI, Szafranek T, Levy NS, Ricklis RM & Levy AP. "Structure-function analysis of the antioxidant properties of haptoglobin". Blood (2001); 98:3693-3698.
[16] Pavlícek Z. & Jaenicke R. "On the mechanism of hemoglobinhaptoglobin complex formation". European Journal of Biochemistry (1971); 18:305-312.
[17] Houston J. B. & Kenworthy KE. "In vitro-in vivo scaling of cyp kinetic data not consistent with the classical Michaelis-Menten model". Drug Metabolism and Disposition (2000); 28:246-254.
[18] Polonovski M. & Jaly M. F. "Existence dans le plasma sanguin d'une substance activant l'action peroxydasique de l'hemoglobine". Comptes Rendus des Seances de la Societe de Biologie et de Ses Filiales. (1938); 129:457-460.
[19] Polonovski M. & Jaly M. F. "Preparation of a new fraction of the plasma proteins, haptoglobin". Comptes Rendus de l'Academie des Sciences 91940); 211:517-519.
[20] Balestrieri M, Cigliano L, De Simone, M. L, Dale B, and Abrescia P. "Haptoglobin inhibits lecithin-cholesterol acyltransferase in human ovarian follicular fluid". Molecular Reproduction and Development (2001); 59:186-191.
[21] Cigliano L, Spagnuolo MS, Dale B, Balestrieri M, and Abrescia P. "Estradiol esterification in the human preovulatory follicle". Steroids (2001); 66:889-896.
[22] Kristiansen M, Graversen J. H, Jacobsen C, Sonne O, Hoffman H. J, Law S. K, and Moestrup S. K. "Identification of the haemoglobin scavenger receptor". Nature (2001); 409:198-201.