Abstract
AbstractWe have prepared a standard of human myoglobin by flat bed isoelectric focusing, to be used in immunological and chemical methods of measurement in clinical biology. Myoglobin was extracted from human psoas or myocardium and then purified by preparative isoelectric focusing in a granulated gel. The purified myoglobin was examined by analytical isoelectric focusing, high performance liquid chromatography (HPLC), immunoelectrophoresis, and two‐dimensional gel electrophoresis. Myoglobin was quantified by three methods: (i) Drabkin's method, and by the determination of iron using (ii) the bathophenanthroline method, and (iii) the atomic emission method. There was good correlation between all three methods. Purified myoglobin was stabilized by conversion to the cyanmetmyglobin form, and stored until use at 4 °C (± 2 °C). or at – 20 °C in the liquid state after addition of ethylene glycol.
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