Hemoglobin heterogeneity in the rabbit: β-112 isoleucine → valine

Shamsuddin, Mir; Rg, Mason; Cohen, Carl; Rg, Tissot; Gr, Honig

doi:10.1016/0003-9861(73)90588-2

Cited by 10 publications

(2 citation statements)

References 9 publications

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“…In rabbits, two a-chain alleles Hba' (29 Val,48 Phe,49 Thr) and Hba" (29 Leu, 48 Leu, 49 Ser) and two /?-chain alleles Hb/?l(52 Asn, 56 Asn,76 Ser,112 Ile) and Hb/?II (52 His,56 Ser,76 Asn,112 Val) have previously been described by analyses of amino acid sequences and amino acid composition of tryptic peptide fragments (Hunter & Munro, 1969;Galizzi, 1970Galizzi, , 1971Shamsuddin et al, 1973;Bricker & Garrick, 1974;Garrick, Bricker & Garrick, 1974a;Garrick et al, 1974b). It is necessary to determine the substitutions between the now reported variants in order to establish whether they are identical with those previously described.…”

Section: Discussionmentioning

confidence: 99%

“…BENCTSSON, U. HELLMAN, I. KkLLMAN A N D C. RANJE AsdSer, 112 Ile/Val) have been shown to be genetically polymorphic (Galizzi, 1970(Galizzi, , 1971Shamsuddin et al, 1973;Bricker & Garrick, 1974;Garrick, Bricker & Garrick, 1974a;Garrick et al, 1974b). Only two common HbS alleles were found when the polymorphic amino acid positions were analysed in more than 300 rabbits (Garrick & Garrick, 1983).…”

Section: Introductionmentioning

confidence: 99%

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Genetic variation of haemoglobin α‐ and βchains in rabbits detected by iso electric focusing and reversed‐phase chromatography

Andersson

Bengtsson

Hellman

et al. 1985

Animal Blood Groups and Biochemical Genetics

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Previous studies on the amino acid sequences and on the amino acid composition of peptides revealed genetic polymorphism both of the haemoglobin a-chain (Hba) and p-chain (Hbp) in rabbits. In this study, rabbit haemolysates were analysed by isoelectric focusing in a narrow p H range (6.7-7.7) and by reversed-phase chromatography. Two variants were found for both Hba and HbP. The two methods detected the same variants in this material. Inheritance data were consistent with the hypothesis that the observed Hba and Hba variants were each controlled by two codominant, autosomal alleles. Haemoglobin polymorphism appears to be frequent in domestic rabbits since both variants of each chain were observed in all the three breeds studied.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Genetic variation of haemoglobin α‐ and βchains in rabbits detected by iso electric focusing and reversed‐phase chromatography

Andersson

Bengtsson

Hellman

et al. 1985

Animal Blood Groups and Biochemical Genetics

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Testing with puromycin for amino acyl trnas that limit the rate of peptide chain extension

Garrick

1978

Mol Cell Biochem

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With puromycin one can recognize when the synthesis of a given protein is dependent on amino acyl tRNA that is present in rate limiting amount. We demonstrate this use of puromycin by its interaction with another inhibitor, L-o-methylthreonine. L-o-methylthreonine lowers the Ile-tRNA concentration in the cell, thereby inhibiting synthesis of proteins containing isoleucine. In certain rabbits, the alpha hemoglobin chain has three isoleucyl residues and the beta chain none. L-o-methylthreonine thus inhibits alpha globin synthesis in intact reticulocytes from these rabbits. When puromycin and L-o-methylthreonine are used together, the two inhibitors synergize in inhibiting alpha globin synthesis. Hence, puromycin is a more effective inhibitor when the Ile-tRNA concentration is lowered. Cycloheximide and sodium fluoride have different modes of action from puromycin. Neither synergizes with L-o-methylthreonine; instead, the interaction is less than additive. We have found that beta chain synthesis in rabbit reticulocytes is more sensitive than alpha to inhibition by puromycin. This difference could reflect either differences in amino acid sequence or tRNA dependent limitations of beta chain elongation. The switch from fetal to adult hemoglobin in humans does not involve changes in limiting amino acyl tRNA because, for cord blood from infants of different developmental ages, the puromycin sensitivity of incorporation into gamma and beta chains remains constant.

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Separation of alpha and beta chains of rabbit globin using SDS-polyacrylamide gel electrophoresis

Wood

Shaeffer

1975

Analytical Biochemistry

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Hemoglobin heterogeneity in the rabbit: β-112 isoleucine → valine

Cited by 10 publications

References 9 publications

Genetic variation of haemoglobin α‐ and βchains in rabbits detected by iso electric focusing and reversed‐phase chromatography

Genetic variation of haemoglobin α‐ and βchains in rabbits detected by iso electric focusing and reversed‐phase chromatography

Testing with puromycin for amino acyl trnas that limit the rate of peptide chain extension

Separation of alpha and beta chains of rabbit globin using SDS-polyacrylamide gel electrophoresis

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