Abstract
Myoglobins (Mb's) were isolated from the dark muscle of mackerel Pneumatophorus japonicus japonicus and sardine Sardinops meianosticta by ammonium sulfate fractionation, Sepiladex G-75 gel filtration, etc. Mb's of both species contained protoheme as the prosthetic group, as do those of other vertebrates. Amino acid analysis revealed that both Mb's include one mole of cysteine/mole, indicating a feature characteristic of fish Mb's. The absorption spectra and alkali resistibility of the Mb's of both species resembled each other and also those from the other sources so far reported. The molecular weight of each Mb was determined to be less than 15, 000, in contrast to those for other sources ranging from 16, 000 to 18, 000. The isoelectric points were as low as 5.8 or 5.9. Mackerel Mb showed autoxidation and thermal stability comparable to those of other fish Mb's, while sardine Mb was less autoxidizable and extremely thermostable; it formed little precipitate even when boiled in 0.2M phosphate buffer at pH 6.7 for 5min.
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