Oxygen affinity of cat hemoglobin

Taketa, F.; Morell, Samuel A.

doi:10.1016/0006-291x(66)90382-2

Cited by 24 publications

(8 citation statements)

References 12 publications

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“…There is no difference in 2,3‐DPG or ATP concentrations in the RBCs of cats with different proportions of HbA:HbB 1,7 . At physiologic concentrations of chloride and carbon dioxide, the oxygen affinities and oxyhemoglobin dissociation curves are the same, irrespective of the relative concentrations of HbA and HbB 1,4,7,34 …”

Section: Discussionmentioning

confidence: 95%

“…1,7 At physiologic concentrations of chloride and carbon dioxide, the oxygen affinities and oxyhemoglobin dissociation curves are the same, irrespective of the relative concentrations of HbA and HbB. 1,4,7,34 In species with high RBC 2,3-DPG concentrations, refrigerator storage is associated with a decrease in red cell 2,3-DPG and a leftward shift of the oxyhemoglobin dissociation curve. There are no reports of the effect of storage on P 50 in any species with low red cell 2,3-DPG.…”

Section: Discussionmentioning

confidence: 99%

“…1,2 In cats, chloride is the major modifier of hemoglobin affinity. [1][2][3][4][5][6] The effect of storage on hemoglobin affinity of cat blood has not been investigated. It was hypothesized because chloride is an inorganic anion that its concentration would not change with storage.…”

Section: Introductionmentioning

confidence: 99%

“…Some species, including cats, have very low concentrations of red cell 2,3‐DPG and it is not a major modifier of hemoglobin affinity for oxygen 1,2 . In cats, chloride is the major modifier of hemoglobin affinity 1–6 . The effect of storage on hemoglobin affinity of cat blood has not been investigated.…”

Section: Introductionmentioning

confidence: 99%

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The effect of storage on the P₅₀ of feline blood

Wong

Haskins

2006

J Vet Emergen Crit Care

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Objective: To determine the effect of storage on the P50 of feline hemoglobin. Design: Prospective, in vitro, laboratory study. Subjects: Venous blood from 4 clinically healthy cats. Measurements: Blood was collected into CPDA‐1 anticoagulant/preservative and maintained at 4°C for 5 weeks. Measurements were made on Days 0, 2, 4, 7, 14, 21, 28, and 35. The blood samples were equilibrated in a tonometer to gas mixtures containing 2.5%, 4%, 5%, or 8% oxygen, with 5% carbon dioxide balance nitrogen; pH was adjusted to 7.4. Chloride, partial pressure of oxygen, and hemoglobin saturation were measured; P50 was calculated. Results: Chloride decreased from 124.3±2.1 to 88.5±1.9 mEq/L immediately after dilution with CPDA‐1, and did not change for the 5 weeks thereafter. The P50 decreased from an average of 35.0±1.2 to between 31 and 32 mmHg after 7 days, and did not change further for 4 weeks thereafter. Conclusions: The decrease in P50 of feline hemoglobin was minor compared with that of blood from species in which 2,3‐diphosphoglycerate (2,3‐DPG) is a major modifier of hemoglobin affinity for oxygen. The decrease in P50 in the present study was attributed to an initial decrease in chloride and a subsequent loss of modest quantities of red cell 2,3‐DPG.

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Section: Discussionmentioning

confidence: 95%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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The effect of storage on the P₅₀ of feline blood

Wong

Haskins

2006

J Vet Emergen Crit Care

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“…Initial studies revealed two variants of cat Hb, namely HbA and HbB, consisting of identical chains but differing in the amino-acid sequence of the chain at positions 1, 4, 139 and 144 (Abbasi & Braunitzer, 1985). Nevertheless, these two isoforms have identical cooperativity and oxygen affinity (Taketa & Morell, 1966;Hamilton & Edelstein, 1974). Further studies of cat Hb polymorphism (Kohn et al, 1998) revealed the existence of six isoforms.…”

Section: Introductionmentioning

confidence: 99%

Structure of liganded T-state haemoglobin from cat (Felis silvestris catus), a low oxygen-affinity species, in two different crystal forms

Moovarkumudalvan

Moorthy

Neelagandan

et al. 2014

Acta Cryst D Biol Crystallogr

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Haemoglobin (Hb) is an iron-containing metalloprotein which plays a major role in the transportation of oxygen from the lungs to tissues and of carbon dioxide back to the lungs. Hb is in equilibrium between low-affinity tense (T) and high-affinity relaxed (R) states associated with its unliganded and liganded forms, respectively. Mammalian species can be classified into two groups on the basis of whether they express `high' or `low' oxygen-affinity Hbs. Although Hbs from the former group have been studied extensively, a more limited number of structural studies have been performed for low oxygen-affinity Hbs. Here, the crystal structure of low oxygen-affinity cat methaemoglobin (metHb) has been solved at 2.0 and 2.4 Å resolution in two different crystal forms. Even though both structures are fully liganded, they unusually adopt a T-state-like quaternary conformation but with several localized R-like tertiary-structural and quaternary-structural features. The study provides atomic-level insights into the ligand-binding properties of this Hb, including its low cooperativity, blunt response to allosteric effectors and low affinity for oxygen, as well as further contributing to the mechanism underlying Hb allostery.

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Biosynthesis of cat hemoglobins: Translation of poly(A)-RNA from animals of various HbA/HbB phenotypes

Kasten‐Jolly

Taketa

1984

Biochem Genet

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The molecular basis for the genetic control of variable proportions of the two hemoglobins in domestic cat blood was investigated. Both major hemoglobins of cat blood, HbA (alpha 2 beta A2) and HbB (alpha 2 beta B2), were synthesized in an mRNA-dependent rabbit reticulocyte system using poly(A)-RNA from cat reticulocyte polysomes as the source of the message. The relative amounts of HbA and HbB synthesized in the system were a function of the HbA/HbB phenotype of the cat from which the reticulocytes and poly(A)-RNA were obtained. Higher ratios of HbA/HbB synthesis were found when the source of poly(A)-RNA was the polysomes from a 90/10 (HbA/HbB) phenotype than when it was from a 50/50 (HbA/HbB) phenotype. These results indicate that the variable proportions of HbA and HbB found in the blood of different members of the cat population result from the genetic control of the relative amounts of functional beta A and beta B mRNA.

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Oxygen affinity of cat hemoglobin

Cited by 24 publications

References 12 publications

The effect of storage on the P₅₀ of feline blood

The effect of storage on the P₅₀ of feline blood

Structure of liganded T-state haemoglobin from cat (Felis silvestris catus), a low oxygen-affinity species, in two different crystal forms

Biosynthesis of cat hemoglobins: Translation of poly(A)-RNA from animals of various HbA/HbB phenotypes

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Oxygen affinity of cat hemoglobin

Cited by 24 publications

References 12 publications

The effect of storage on the P50 of feline blood

The effect of storage on the P50 of feline blood

Structure of liganded T-state haemoglobin from cat (Felis silvestris catus), a low oxygen-affinity species, in two different crystal forms

Biosynthesis of cat hemoglobins: Translation of poly(A)-RNA from animals of various HbA/HbB phenotypes

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The effect of storage on the P₅₀ of feline blood

The effect of storage on the P₅₀ of feline blood