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The structure of Mus musculus bactrianus hemoglobin. I. Isolation and preliminary characterization of the globin chains
Authors:Giovanni Vulpis  Sandro Quaggia
Affiliation:(1) Laboratorio di Radiobiologia Animale, C.S.N. della Casaccia, Comitato Nazionale Energia Nucleare, Rome, Italy
Abstract:The minor component of Japanese dancing mice hemoglobin, which runs more slowly on electrophoresis, differs from its major component in the non-agr chains. The alkaline denaturation results show that the x chains are more alkali labile than agr and beta chains. Globin electrophoresis provides evidence that the charge difference between the major and minor components is located in non-agr chains.This paper was partly presented at the First Meeting of the European Division of the International Society of Haematology, Milan, September 1971.
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