Haemoglobins of Sheep

Beale, D.; Lehmann, H.; Drury, A. N.; Tucker, Elizabeth M.

doi:10.1038/2091099a0

Cited by 41 publications

(17 citation statements)

References 19 publications

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“…Van Vliet and Huisman (5) showed that Hb A is entirely replaced during severe anemia by a new hemoglobin type which they named Hb C. In heterozygous Hb AB sheep the relative proportion of Hb B remains constant during anemia; homozygous Hb B sheep do not show any change. These hemoglobins all possess the same alpha chain but differ at multiple amino sites in their beta chains (6)(7)(8)(9)(10). Thus the conversion from Hb A to Hb C formation is primarily one of a reciprocal relationship in the activity of the genes directing the synthesis of betaA and beta0 chains.…”

Section: Abstract This Investigation Is Concernedmentioning

confidence: 99%

Erythropoietic kinetics in sheep studied by means of induced changes in hemoglobin phenotype

Gabuzda¹,

Schuman²,

Silver³

et al. 1968

J. Clin. Invest.

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Section: Abstract This Investigation Is Concernedmentioning

confidence: 99%

Erythropoietic kinetics in sheep studied by means of induced changes in hemoglobin phenotype

Gabuzda¹,

Schuman²,

Silver³

et al. 1968

J. Clin. Invest.

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“…2(b), 2((7)] produced two interaction products, the slower interaction product having the same mobility in each case. The results of other workers (Beale et al 1966) indicate that the fast interaction products have the composition a:~anygv and a:ganyga p and the slow interaction products a:~v,8~an and a:~ap,8~an.…”

Section: (D)mentioning

confidence: 58%

The Haemoglobins of a Sheep-Goat Hybrid Foetus and those of the Parent Species

Bailey¹,

Alexander²,

Williams³

1967

Aust. Jnl. Of Bio. Sci.

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SummaryElectrophoretic examination of the haemoglobins of a sheep-goat hybrid foetus indicated the presence of haemoglobins found in the foetuses of the parent species only. No interaction products were found.In vitro "hybridization" experiments indicate that the difference in electrophoretic mobility between sheep A, sheep B, goat A, goat F, and sheep F haemoglobins is due to a difference in the non-ex-portion of the haemoglobin molecules. The absence of electrophoretically detectable haemoglobin interaction products in the hybrid foetus is explained by the finding that the ex-polypeptides of the parent species are electrophoretically indistinguishable.

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“…Hb-C becomes a major haemoglobin in animals severely anaemic from blood loss by replacing Hb-A but not Hb-B. The s-chain ofHb-C is composed of 141 residues and differs from the pA-chain by at least 16 residues and from the ,B-chain by at least 21 residues (Beale et al 1966;Boyer et al 1966Boyer et al , 1967Wilson et al 1966). A similar phenomenon is also observed in the domestic goat (Huisman, Adams, Dimmock, Edwards & Wilson, 1967 (Huisman, van Viet & Sebens, 1958;Meyer, 1967) have indicated a marked variability in several species.…”

Section: Originatedmentioning

confidence: 99%

“…The primary structures of the ,-chains of the two adult sheep haemoglobin types, designated as Hb-A* and Hb-B, have recently been determined (Beale, Lehmann, Drury & Tucker, 1966;Boyer et al 1966Boyer et al , 1967Huisman, Reynolds, Dozy & Wilson, 1965; Wilson, Edwards, McDaniel, Dobbs & Huisman, 1966). The two polypeptide chains are each composed of 145 residues; they differ by at least seven residues, which are located in positions 50, 58, 75, 76, 120, 129 and 144, counted from the N-terminal end (indicated as position 2).…”

Section: Originatedmentioning

confidence: 99%

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Studies of haemoglobin types in barbary sheep (Ammotragus lervia)

1968

Biochemical Journal

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1. Two haemoglobin types, haemoglobins Amm-C and Amm-B, were observed in five Barbary sheep (Ammotragus lervia). One animal was homozygous for haemoglobin Amm-C, a second was homozygous for haemoglobin Amm-B, and three were heterozygous for both. 2. Amino acid analyses of the globin from haemoglobin Amm-B showed that this type was related to, but not identical with, haemoglobin B of the domestic sheep. 3. The β-chain of haemoglobin Amm-C was found to be composed of 141 amino acid residues. Its amino acid composition differed from that of the βC-chain of the anaemic domestic sheep in at least 14 residues. The Amm-βC-chain contained one isoleucyl residue. 4. The amino acid compositions of tryptic peptides T-1, T-2, T-13 and T-14 of the Amm-βC-chain were similar to those of the sheep βC-chain. Peptides T-3, T-4, T-6, T-7, T-8, T-11 and T-15 were the same as the corresponding peptides of the sheep βA- and βC-chains. Peptide T-5 and to a smaller extent peptide T-9 resembled the corresponding peptides of the sheep βA-chain, and peptide T-10 was identical with peptide γT-10 of sheep haemoglobin F. Peptide T-12 was not recovered. 5. The results of these investigations were interpreted as being indicative that the structural Amm-βC-gene is closely related to the βC-gene of sheep, from which through domestication the present domestic sheep originated.

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Haemoglobins of Sheep

Cited by 41 publications

References 19 publications

Erythropoietic kinetics in sheep studied by means of induced changes in hemoglobin phenotype

Erythropoietic kinetics in sheep studied by means of induced changes in hemoglobin phenotype

The Haemoglobins of a Sheep-Goat Hybrid Foetus and those of the Parent Species

Studies of haemoglobin types in barbary sheep (Ammotragus lervia)

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