血合筋肉の化学的研究-XI : マグロミオグロビンのアミノ酸組成

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Amino acid composition of myoglobin (Mb) of tuna, Thunnus orientalis, was determined. The globin, prepared from the thrice-recrystallized Mb, was hydrolyzed with 20% HCl for 24 hrs. and analyzed by the method of STEIN & MOORE7). The hydrolyzate for tryptophan was prepared after GREENE6) and analyzed similarly. Cystine and/or cysteine were determined by the method of SCHRAM5). The elution curves are shown in Fig. 1. The amino acid composition of tuna Mb was shown in Table 1, together with that of hemoglobin (Hb) of tuna, T. thynnus13), and that of mammalian pigments. Distinct differences were discerned between Mb and Hb of tuna, as seen in the case of horse11) or human14). Most of relative quantitative differences of corresponding amino acids, however, were similar to those observed in the cases of mammalia, except for leucine, methionine, and histidine, etc. Next the following differences are pointed out by comparing amino acid composition of tuna Mb to that of mammalian Mbs: (1) Amongst monoamino-monocarboxylic amino acid, alanine is most prevailing in tuna, whereas leucine in mammalia. (2) Tuna Mb contains one cysteine residue, the absence of which has been reported for mammalian Mbs (cf. Table 1 and ROSSI-FANELLI et al.14)). (3) In tuna Mb, glutamic acid and basic amino acids are considerably poor. The percentage distribution of groups in tuna Mb and the others are shown in Table 2. Tuna Mb is scant in free anionic and cationic groups. Accordingly the total of both groups of tuna Mb is less than that of mammalian Mb and rather comparable to its Hb. However, the difference between two groups reveals the more or less basic nature of the globin. The total of polar groups of tuna Mb was found also to be low as the total of ionic groups is, which will account for the relatively low solubility of tuna Mb reported before2).

血合筋肉の化学的研究-XI : マグロミオグロビンのアミノ酸組成

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