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Isolation of Two Myoglobins from Horse-heart Extracts and the Determination of the Molecular Weight of the Main Component


THE method developed by Boardman and Partridge1 for the separation of hæmoglobins on columns of the ion-exchange resin, ‘Amberlite IRC-50’ (XE–64), has been applied to the purification of horse carbon monoxide myoglobin, with the result that two carbon monoxide myoglobins were isolated from extracts of horse heart. The component carbon monoxide myoglobin (B) was present to the extent of about 10 per cent of the main myoglobin fraction, carbon monoxide myoglobin (A). Each fraction was shown to be homogeneous in the ultracentrifuge, and when examined in a Hilger ‘Uvispek’ spectrophotometer each gave an absorption spectrum typical of carbon monoxide myoglobin. The molecular weight of the main component was determined from measurements of osmotic pressure2 and a detailed amino-acid analysis was carried out by the procedure of Moore and Stein3.

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BOARDMAN, N., ADAIR, G. Isolation of Two Myoglobins from Horse-heart Extracts and the Determination of the Molecular Weight of the Main Component. Nature 177, 1078–1079 (1956).

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