Studies on the reaction of haptoglobin with haemoglobin and haemoglobin chains

Chiancone, Emilia; Alfsen, Annette; Ioppolo, Carmela; Vecchini, Paola; Agró, Alessandro Finazzi; Wyman, Jeffries; Antonini, Eraldo

doi:10.1016/0022-2836(68)90258-1

Cited by 82 publications

(47 citation statements)

References 13 publications

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“…The binding characteristics of the Aga-Hp material was determined by addition of increasing amounts of 3H-labelled samples of H b A or of isolated aH or iso- Our results are similar to those previously reported using Hp in solution [21] and indicates that Hp covalently linked to Sepharose 4B preserves its specific characteristics of binding.…”

Section: Binding Characteristics Of Aga-hpsupporting

confidence: 87%

Globin‐Chain Affinity Chromatography on Sepharose‐Haptoglobin a New Method of Study of Hemoglobin Synthesis in Reticulocytes, in Bone Marrow and in Colonies of Erythroid Precursors

Tsapis

Hinard

Testa

et al. 1980

European Journal of Biochemistry

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In the present work we have developed an affinity chromatography system, using haptoglobin bound covalently to Sepharose 4B, to purify hemoglobin from soluble non‐heme proteins. Sepharosehaptoglobin specifically binds hemoglobin. It exhibits the same characteristics in its interactions with hemoglobin and α or β hemoglobin chains as does haptoglobin in solution. Globin chains can be eluted from the Sepharose‐haptoglobin after removal of the heme. This method has allowed accurate measurements of globin‐chain synthesis in blood and bone marrow samples and in culture of early erythroid precursors.

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Section: Binding Characteristics Of Aga-hpsupporting

confidence: 87%

Globin‐Chain Affinity Chromatography on Sepharose‐Haptoglobin a New Method of Study of Hemoglobin Synthesis in Reticulocytes, in Bone Marrow and in Colonies of Erythroid Precursors

Tsapis

Hinard

Testa

et al. 1980

European Journal of Biochemistry

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“…Plasma contains haptoglobin [7], a high-affinity binder of oxyhemoglobin and inhibitor of auto-oxidation; iron-and heme-binding proteins such as transferrin, albumin, and hemopexin; and antioxidants such as vitamin E and ascorbic acid. However it is generally agreed that these systems are not sufficient to protect against hemoglobin-mediated oxidative cell and tissue damage during increased extravascular hemolysis and general hemolytic pathologic disorders.…”

Section: Introductionmentioning

confidence: 99%

Up-regulation of α1-microglobulin by hemoglobin and reactive oxygen species in hepatoma and blood cell lines

Olsson

Maria

Olofsson

et al. 2007

Free Radical Biology and Medicine

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“…It seems generally accepted [2,[4][5][6]151, that the reactive unit in the Hb-Hp interaction is the ap-dimer of Hb. Assuming the Hp-(o~/?)…”

Section: Discussionmentioning

confidence: 99%

On the Mechanism of Hemoglobin‐Haptoglobin Complex Formation

Pavlı́ček

Jaenicke

1971

European Journal of Biochemistry

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In order to elucidate the mechanism of complex formation between human haptoglobin, Hp II, and bovine hemoglobin, Hb, measurements of the peroxidase activity and histidine determinations, as well as spectrophtometric and optical rotatroy dispersion titration experiments were performed. Following the raaction by slowly mixing the constituents of the complex in small portinos, the geometry of the complex turns out to depend on the sequence of mixing of the reactants. Adding Hb to Hp, a final complex Hb2→ Hp is formed. Teh inverse sequence of mixing leads to a complex of identical composition (Hp → Hb2), but different arrangement of the constituents, as shown by differences in the accessibility of histidine residues in both types of the complex. As suggested by the comparison of the histidine balance of both complexes, Hb2→ Hp may be described by the combination of αβ‐dimers of Hb with Hp (Hp (αβ)4), while Hp → Hb2 corresponds to the complex with two Hb tetramers (Hp(α2β2)2). Investigating the saturation process of complex formation in greater detail by spectrophtometric titration and optical rotatory dispersion, intermediary complexes are observed which prove the mechanism of complex formation to be a consecutive association process. Both series of complexes, Hp → Hb and Hb → Hp, seem to generate closely related configurations characterized by similar spectral and functional properties.

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Studies on the reaction of haptoglobin with haemoglobin and haemoglobin chains

Cited by 82 publications

References 13 publications

Globin‐Chain Affinity Chromatography on Sepharose‐Haptoglobin a New Method of Study of Hemoglobin Synthesis in Reticulocytes, in Bone Marrow and in Colonies of Erythroid Precursors

Globin‐Chain Affinity Chromatography on Sepharose‐Haptoglobin a New Method of Study of Hemoglobin Synthesis in Reticulocytes, in Bone Marrow and in Colonies of Erythroid Precursors

Up-regulation of α1-microglobulin by hemoglobin and reactive oxygen species in hepatoma and blood cell lines

On the Mechanism of Hemoglobin‐Haptoglobin Complex Formation

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