Increase of Peroxidase Activity of Haptoglobin (2-2)-Hemoglobin at Pathologic Temperature and Presence of Antibiotics
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).
[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.
[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.
@article{"International Journal of Medical, Medicine and Health Sciences:62560", author = "M Tayari and SZ Moosavi-nejad and A Shabani and M Rezaei Tavirani", title = "Increase of Peroxidase Activity of Haptoglobin (2-2)-Hemoglobin at Pathologic Temperature and Presence of Antibiotics", 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.", volume = "4", number = "9", pages = "492-7", }
