Abstract
The purification and characterization of seal meat myoglobin after aqueous extraction of hemoproteins from muscle tissues was investigated. Of the 59 mg/g total hemoproteinsin seal meat, only 27% of its myoglobin content was recovered by the commonly used buffer precipitation method. Similar observations were made for the content of myoglobin in other muscle tissues. Thus, quantification of myoglobin by the phosphate precipitation method is inaccurate. The amino acid composition of harp seal myoglobin was similar to those of gray and harbor seals as well as that of sperm whale
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