Abstract
RUMEN1 isolated from seal, by chromatography on CM-cellulose in tris buffer at pH 8.5, five myoglobins all with the same iron content and the same N-terminal, but showed differences in isoelectric points. Åkeson and Theorell2 isolated, from horse muscle, three myoglobins with similar amino-acid compositions but had charge differences. Sperm whale myoglobin was fractionated by Edmundson and Hirs3, on ‘IRC-50’ into four components, using citrate–chloride buffer at pR 5.86–5.88. However, they encountered zone tailing which, as they pointed out, might have masked the presence of minor components, We have resolved crystalline sperm whale myoglobin into at least twelve components by chromatography. Some properties of these components have been investigated. These included their amino-acid compositions, spectral and electrophoretic behaviour, their molecular weights, and their antigenic character.
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ATASSI, M. Properties of Components of Myoglobin of the Sperm Whale. Nature 202, 496–498 (1964). https://doi.org/10.1038/202496a0
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DOI: https://doi.org/10.1038/202496a0
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