鶏の筋肉組織におけるミオグロビン成分および含量の比較

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Chicken skeletal myoglobin purified by DEAE-Sephadex chromatography revealed heterogeneity, showing three myoglobin bands by acrylamide disc gel electrophoresis and two precipitin lines by double immunodiffusion against anti-chicken skeletal myoglobin; the one fused with the line formed with a major myoglobin (Mb I) and the other fused with the line formed with one of minor myoglobins (Mb II). The skeletal Mb II was not identical to Mb I in immunochemical reaction. Two precipitin lines identical to Mb I and Mb II were formed in all the limb muscles diffused against the anti-skeletal myoglobin, except that the mm. adductores, the red portion of m. pectoralis superficialis, the cardiac and the gizzard muscle formed a single line fusing with the line formed with Mb I. The white portion of m. pectoralis superticialis and the m. pectoralis profundus did not cross-react with the anti-skeletal myoglobin. Myoglobin concentration determined for Mb I and Mb II by single radial immunodiffusion was undetectable in the white m. pectoralis superficialis and extremely low in the m. pectoralis profundus. In the pelvic limb muscles, a significantly large amount of Mb I was contained in the mm. vastus intermedius, adductores, gastrocnemius caput mediale and tibialis posterior, which contained an extremely small amount of Mb II or no Mb II, whereas the mm. biceps brachii, triceps brachii, biceps femoris and semimembranosus with a significantly small amount of Mb I contained Mb II in a high level. There was a negative correlation between the contents of Mb I and Mb II in the individual limb muscles. The cardiac and the gizzard muscles contained only Mb I in relatively high level, and in extremely large amounts, respectively. These quantitative results were consistent with the observation with the immunochemical reaction. Thus, Mb II seemed to be a specific component contained only in the skelefal muscle.
社団法人日本獣医学会の論文
1978-08-25

鶏の筋肉組織におけるミオグロビン成分および含量の比較

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