Effect of 2,3-diphosphoglycerate on the cooperativity in oxygen binding of human adult hemoglobin

Tyuma, Itiro; Shimizu, Katsuhiko; Imai, Katsunori

doi:10.1016/0006-291x(71)90770-4

Cited by 108 publications

(30 citation statements)

References 9 publications

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“…The erythrocyte mass of a carrier of Hb Rahere was within the normal range, as it was in our patients, suggesting that oxygen transport is normal in both hemoglobinopathies. The dissociation curve of our proband was not biphasic (an unexpected finding, for the major effect of DPG is exerted at low oxygen saturations [31]), and oxygen delivery must be maintained by nonhematopoietic adjustments.…”

mentioning

confidence: 56%

Postsynthetic deamidation of hemoglobin Providence (beta 82 Lys replaced by Asn, Asp) and its effect on oxygen transport.

et al. 1977

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A B S T R A C T Carriers of hemoglobin Providencehave three types of ,3 chain in their hemolysates. The two abnormal chains have asparagine (Providence N, Prov N) or aspartic acid (Providence D) at position 83 82, instead of lysine. In vitro, only two 18 chains are synthesized by reticulocytes of carriers, , and "V N. In vivo studies showed that the specific activity of Providence N was initially 10-fold higher than that of Providence D; the specific activities of the two labeled hemoglobins were approximately equal 5 wk after injection of isotope.Oxygen affinity of carriers' blood was somewhat increased, but they were not polycythemic. The affinity of the purified hemoglobins Providence was decreased. Addition of 2, 3 diphosphoglycerate had little effect on the affinity of either hemoglobin component, and addition of inositol hexaphosphate produced no change in the affinity of Providence D.These studies demonstrate that Providence N is deamidated to Providence D during the life span of the erythrocyte, and suggest this finding may represent only an easily observed prototype of posttranslational modification of proteins in general.Depite an abnormal P50 of the blood, oxygen transport is probably normal in carriers of the abnormal hemoglobins.

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confidence: 56%

Postsynthetic deamidation of hemoglobin Providence (beta 82 Lys replaced by Asn, Asp) and its effect on oxygen transport.

et al. 1977

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“…Experimentally KT and KR are taken to be K, and K4, the first and fourth oxygen binding constants of hemoglobin. These can be estimated from the two ends of the oxygen binding curve and give AG = 3.6 kcal mol-1 for hemoglobin (27). Cobalt hemoglobin.…”

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confidence: 99%

Resonance Raman Spectra of Cobalt-Substituted Hemoglobin: Cooperativity and Displacement of the Cobalt Atom upon Oxygenation

Woodruff

Spiro

Yonetani

1974

Proc. Natl. Acad. Sci. U.S.A.

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The resonance Raman spectra of oxy and deoxy cobalt-substituted hemoglobin (CoHb) are reported. Comparison of these spectra to those of hemoglobin, methemoglobin, cytochrome c, and model cobalt porphyrin complexes suggests that the displacement of the cobalt atom upon oxygenation of CoHb is no greater than the out-of-plane distance in five-coordinate Co(II) porphyrins, 0.15 A. Combining this distance with the expected contraction of the cobalt-histidine bond, Ibers has estimated a maximum displacement of 0.37 A for the proximal histidine with respect to the heme plane upon oxygenation, about one-third the corresponding distance estimated for iron hemoglobin. The free energy of cooperativity for cobalt hemoglobin is also estimated to be onethird that of iron hemoglobin. These results are therefore consistent with Hopfield's distributed energy model, which predicts proportionality between proximal histidine displacement and the free energy of cooperativity. By implication they support Perutz's trigger mechanism for cooperativity.

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“…5). In contrast to most vertebrate Hbs where organic phosphates primarily reduce the O 2 association constant of the low affinity, tense state of the Hb molecules (K T ) (55,62) thus increasing the free energy of cooperativity (⌬G), ATP also decreases the association constant of the high-affinity relaxed state (K R ) and reduces ⌬G (Table 2). However, the K R values need to be viewed with caution due to difficulties in measuring the last few percent saturation of the oxygenation curve (37).…”

Section: Hbmentioning

confidence: 99%

Novel mechanism for high-altitude adaptation in hemoglobin of the Andean frogTelmatobius peruvianus

Weber

Ostojic²,

Fago

et al. 2002

American Journal of Physiology-Regulatory, Integrative and Comp

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In contrast to birds and mammals, no information appears to be available on the molecular adaptations for O2 transport in high-altitude ectothermic vertebrates. We investigated Hb of the aquatic Andean frog Telmatobius peruvianus from 3,800-m altitude as regards isoform differentiation, sensitivity to allosteric cofactors, and primary structures of the ␣-and ␤-chains, and we carried out comparative O2-binding measurements on Hb of lowland Xenopus laevis. The three T. peruvianus isoHbs show similar functional properties. The high O2 affinity of the major component results from an almost complete obliteration of chloride sensitivity, which correlates with two ␣-chain modifications: blockage of the NH2-terminal residues and replacement by nonpolar Ala of polar residues Ser and Thr found at position ␣131(H14) in human and X. leavis Hbs, respectively. The data indicate adaptive significance of ␣-chain chloride-binding sites in amphibians, in contrast to human Hb where chloride appears mainly to bind in the cavity between the ␤-chains. The findings are discussed in relation to other strategies for high-altitude adaptations in amphibians.amphibians; chloride binding; hypoxia; organic phosphates; oxygen transport HOW IS OXYGEN TRANSPORT to metabolizing tissues secured at high altitude? In contrast to intensive investigations in birds and mammals (7,39,59), the molecular strategies for O 2 transport in high-altitude ectothermic vertebrates remain unexplored, despite greater variations in environmental conditions (temperature, pH, O 2 tension, etc.) and lesser capacities for homeostatic regulation of internal physical and chemical conditions compared with homeothermic vertebrates and a long-standing interest in high-altitude aquatic amphibians (1, 24).The anuran genus Telmatobius (that variously is referred to as frogs or toads) occurs in the Andes mountains at altitudes from 2,000 to over 4,000 m (14) where aerial O 2 tensions fall from ϳ159 mmHg at sea level to ϳ92 mmHg. The hypoxic stress is compounded in aquatic species, particularly at night when photosynthetic activity in the ponds ceases (21). T. culeus found in Lake Titicaca at 3,812 m has reduced, poorly developed lungs but exhibits compensatory physiological and behavioral adaptations (24) that include an "oversized," folded skin, which is penetrated by cutaneous capillaries and ventilated by "bobbing" behavior under hypoxia, and small erythrocytes and higher erythrocyte counts, blood-O 2 affinities, and O 2 -carrying capacities than anurans living at sea level (24). Subspecies of Bufo spinulosus living at sea level and at 3,100 to 4,100 m in the Andes analogously exhibit increasing blood-O 2 affinities with altitude (43).The O 2 affinity of blood is a product of the intrinsic O 2 affinity of the Hb molecules and the erythrocytic effectors that modulate Hb-O 2 affinity. Compared with mammals that use 2,3-diphosphoglycerate (DPG) and fish that use ATP (often in conjunction with the more potent effector guanosine triphosphate) (60) as organic O 2 -affinity modulat...

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Effect of 2,3-diphosphoglycerate on the cooperativity in oxygen binding of human adult hemoglobin

Cited by 108 publications

References 9 publications

Postsynthetic deamidation of hemoglobin Providence (beta 82 Lys replaced by Asn, Asp) and its effect on oxygen transport.

Postsynthetic deamidation of hemoglobin Providence (beta 82 Lys replaced by Asn, Asp) and its effect on oxygen transport.

Resonance Raman Spectra of Cobalt-Substituted Hemoglobin: Cooperativity and Displacement of the Cobalt Atom upon Oxygenation

Novel mechanism for high-altitude adaptation in hemoglobin of the Andean frogTelmatobius peruvianus

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