Crystalline Human Myoglobin: Some Physicochemical Properties and Chemical Composition

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Abstract
Human myoglobin crystals are long, very thin needles, tied in sub parallel bundles or in radiated, fibrous spheroidal masses. Crystals of metmyoglobin are double-refracting. The Fe content is 0.34%, the N content 16.5%. Spectrophotometric detns. gave maxima of 5,815 A and 5,426 A for the a and B absorption bands of oxymyoglobin, respectively. Myoglobin is relatively stable in an alkaline medium. While in 0.4 N NaOH human oxyhemoglobin is rapidly transformed to hemochromogen; the oxymyoglobin still presents the 2 typical [alpha] and [beta] bands of oxymyoglobin. Myoglobins from different animals behave differently toward alkali. The chem. composition of myoglobin is different from that of hemoglobin. The most conspicuous differences are in the arginine and lysine content and also in the monoamino acids. Myoglobin of different animal spp. contains about half as much arginine and twice as much lysine as Hb of the same animal and the total amt. of basic amino acid radicals is greater in myoglobin than in Hb.