Abstract
Starch gel electrophoretic and ultracentrifuge methods failed to demonstrate any differences between the hemoglobins of mice of the Shanghai and HBBP/Cag strains and crosses among these strains. The apparent identity of these hemoglobins is thought to stem from the contribution of Asian mice to the British mouse fancy from which the laboratory strains having Hbb-p in part descerd. Maleate buffer of pH 7 or above can be used to prevent the formation of disulfide-bridged dimers of mouse hemoglobins. However, the minor electrophoretic bands of Hbb-p and Hbb-d react with approximately twice as much maleate as the major bands of each of these hemoglobins, although the minor bands like the major contain only one free cysteine group per β chain. This can be explained by the alkylation of the μ-amino of lysine residue β76, but some evidence for the alkylation of histidine in the minor band of Hbb-p is also presented.
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Morton, J.R., Tobin, G. Experiments with β-chain variants of the hemoglobin of Mus musculus . Biochem Genet 15, 101–108 (1977). https://doi.org/10.1007/BF00484552
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DOI: https://doi.org/10.1007/BF00484552