Hemoglobin heterogeneity in the cat

Taketa, F.; Smits, Miriam; Lessard, James L.

doi:10.1016/0006-291x(68)90438-5

Cited by 19 publications

(5 citation statements)

References 5 publications

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“…In analogy with the domestic cat, products of each of the two β-globin genes HBB/D and HBB are incorporated into two distinct Hb isoforms, HbA and HbB, respectively, which share the same α-chain subunit encoded by the two identical HBA genes (Abbasi and Braunitzer, 1985;Taketa et al, 1968) (Fig. 2).…”

Section: Low Levels Of Structural Variation Among Felid Hbsmentioning

confidence: 99%

Genetically based low oxygen affinities of felid hemoglobins: lack of biochemical adaptation to high-altitude hypoxia in the snow leopard

Janečka

Nielsen

Andersen

et al. 2015

Journal of Experimental Biology

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Genetically based modifications of hemoglobin (Hb) function that increase blood-O 2 affinity are hallmarks of hypoxia adaptation in vertebrates. Among mammals, felid Hbs are unusual in that they have low intrinsic O 2 affinities and reduced sensitivities to the allosteric cofactor 2,3-diphosphoglycerate (DPG). This combination of features compromises the acclimatization capacity of blood-O 2 affinity and has led to the hypothesis that felids have a restricted physiological niche breadth relative to other mammals. In seeming defiance of this conjecture, the snow leopard (Panthera uncia) has an extraordinarily broad elevational distribution and occurs at elevations above 6000 m in the Himalayas. Here, we characterized structural and functional variation of big cat Hbs and investigated molecular mechanisms of Hb adaptation and allosteric regulation that may contribute to the extreme hypoxia tolerance of the snow leopard. Experiments revealed that purified Hbs from snow leopard and African lion exhibited equally low O 2 affinities and DPG sensitivities. Both properties are primarily attributable to a single amino acid substitution, β2His→Phe, which occurred in the common ancestor of Felidae. Given the low O 2 affinity and reduced regulatory capacity of feline Hbs, the extreme hypoxia tolerance of snow leopards must be attributable to compensatory modifications of other steps in the O 2 -transport pathway.

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Section: Low Levels Of Structural Variation Among Felid Hbsmentioning

confidence: 99%

Genetically based low oxygen affinities of felid hemoglobins: lack of biochemical adaptation to high-altitude hypoxia in the snow leopard

Janečka

Nielsen

Andersen

et al. 2015

Journal of Experimental Biology

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“…The alkyl and aryl mercurials are one of the more specific classes of chemical reagent for thiol groups in proteins (Webb, 1966b). Cat haemoglobin has eight thiol groups in each tetramer titratable with p-chloromercuribenzoate (Taketa et al, 1968); the effect of preincubation of cat haemoglobin with increasing concentrations of phenylmercuric acetate on the Vol. 177 Bound triethyltin (mol/mol of haemoglobin) Fig.…”

Section: Resultsmentioning

confidence: 99%

Triethyltin binding to cat haemoglobin. Evidence for two chemically distinct sites and a role for both histidine and cysteine residues

Elliott¹,

Aldridge²,

Bridges³

1979

Biochemical Journal

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Triethyltin binding to cat haemoglobin was measured after pretreatment of the protein with diethyl pyrocarbonate at pH 6.0,iodoacetamide or phenylmercuric acetate or by photo-oxidation in the presence of Methylene Blue. The pentaco-ordinate nature of the binding of triethyltin to cat haemoglobin is confirmed by the inability of intramolecularly pentaco-ordinate tin compounds to compete. Consideration of the symmetry of the haemoglobin molecule in the light of the above results suggests that a unique arrangement of histidine and cysteine residues is required for the binding of triethyltin. The effects of treatment with diethyl pyrocarbonate of other preparations which bind triethyltin (rat liver supernatant, a fraction from rat liver mitochondria and rat brain myelin) were determined and shown to be complex.

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“…There are species variations in Hb, however. In this context, cat Hb is noticeable in having 8-10 readily oxidizable sulphydryl groups [9,10] whilst most other species including humans and dogs have only two main ones, represented by the highly conserved β93 cysteines [11,12]. Cat Hb also readily dissociates from the usual tetrameric form to dimers [13] which have a greater tendency for autoxidation [14].…”

Section: Dog and Cat Red Cellsmentioning

confidence: 99%

“…They are also found in the circulation of healthy cats, however, at up to 5-10 % red cells, presumably because of their greater number of oxidative sites in Hb and impaired red cell antioxidant defence, together with the poor ability of the non-sinusoidal feline spleen to remove Heinz body-containing red cells [15]. Cats also have two main Hbs A and B [9,16]. HbA is most prevalent in domestic short-and long-haired cats have HbA (98 %) but a few breeds have greater levels of HbB (eg 10 % Persians and 14 % in Abyssinians, with as much as 50 % in Devon Rexs) and geographically to occur {eg [17]}.…”

Section: Dog and Cat Red Cellsmentioning

confidence: 99%

Oxidative Stress and Haemolytic Anaemia In Dogs and Cats: A Comparative Approach

2019

Integr J Vet Biosci

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Hemoglobin heterogeneity in the cat

Cited by 19 publications

References 5 publications

Genetically based low oxygen affinities of felid hemoglobins: lack of biochemical adaptation to high-altitude hypoxia in the snow leopard

Genetically based low oxygen affinities of felid hemoglobins: lack of biochemical adaptation to high-altitude hypoxia in the snow leopard

Triethyltin binding to cat haemoglobin. Evidence for two chemically distinct sites and a role for both histidine and cysteine residues

Oxidative Stress and Haemolytic Anaemia In Dogs and Cats: A Comparative Approach

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