The ferric form of reindeer hemoglobin (Rangifer tarandus tarandus) has been crystallized in an orthorhombic crystalline form from polyethylene glycol solutions, at pH 8.2. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit cell edges a = 84.2 A, b = 59.9 A, c = 119.5 A; one hemoglobin tetramer is contained in the asymmetric unit. The crystals diffract X-rays to a limit spacing of 3.0 A. Inspection of amino acid sequences in the N-terminal region of beta-chains, and analysis of hemoglobin three-dimensional models, allows one to rationalize, on a molecular basis, the reduced O2 affinity and the decreased effect of organic phosphates observed in ruminant hemoglobins. By analogy, the analysis is extended to birds and reptiles, whose hemoglobin beta-chains display, as in ruminants, the deletion of the N-terminal residue and a methionine at the NA2 position.

Conti, E., Casale, E., Ascenzi, P., Coletta, M., Condo', S.g., Merli, A., et al. (1992). Structural study and preliminary crystallographic data for the hemoglobin from reindeer (Rangifer tarandus tarandus). BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 187(2), 1063-1070.

Structural study and preliminary crystallographic data for the hemoglobin from reindeer (Rangifer tarandus tarandus)

COLETTA, MASSIMILIANO;CONDO', SAVERIO GIOVANNI;
1992-09-16

Abstract

The ferric form of reindeer hemoglobin (Rangifer tarandus tarandus) has been crystallized in an orthorhombic crystalline form from polyethylene glycol solutions, at pH 8.2. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit cell edges a = 84.2 A, b = 59.9 A, c = 119.5 A; one hemoglobin tetramer is contained in the asymmetric unit. The crystals diffract X-rays to a limit spacing of 3.0 A. Inspection of amino acid sequences in the N-terminal region of beta-chains, and analysis of hemoglobin three-dimensional models, allows one to rationalize, on a molecular basis, the reduced O2 affinity and the decreased effect of organic phosphates observed in ruminant hemoglobins. By analogy, the analysis is extended to birds and reptiles, whose hemoglobin beta-chains display, as in ruminants, the deletion of the N-terminal residue and a methionine at the NA2 position.
16-set-1992
Pubblicato
Rilevanza internazionale
Articolo
Sì, ma tipo non specificato
Settore BIO/10 - BIOCHIMICA
English
Con Impact Factor ISI
Crystallization; Molecular Structure; Animals; Ferric Compounds; X-Ray Diffraction; Chemistry, Physical; Humans; Hydrogen-Ion Concentration; Diphosphoglyceric Acids; Reindeer; Binding Sites; Macromolecular Substances; Physicochemical Phenomena; 2,3-Diphosphoglycerate; Hemoglobins; Spectrophotometry
Conti, E., Casale, E., Ascenzi, P., Coletta, M., Condo', S.g., Merli, A., et al. (1992). Structural study and preliminary crystallographic data for the hemoglobin from reindeer (Rangifer tarandus tarandus). BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 187(2), 1063-1070.
Conti, E; Casale, E; Ascenzi, P; Coletta, M; Condo', Sg; Merli, A; Giardina, B; Bordo, D; Bolognesi, M
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/54677
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