Studies on the Proteins of sheil-Fish VI Paper-Electrophoretic Behavior of Myosin Fraction of Adductor Muscle of Clam, Meretrix meretrix

In this report, characterization of protein of myosin fraction of clam muscle was studied with paper-electrophoresis. Paper-electrophoresis was conducted at ionic strength 0.1, 0.25 and 0.35, and at pH 7.2-7.5, about myosin A and myosin B fractions of adductor muscle of clam extracted with Weber-Eds...

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Bibliographic Details
Published inThe Japanese Journal of Nutrition and Dietetics Vol. 17; no. 3; pp. 107 - 110
Main Author Baba, Haruo
Format Journal Article
LanguageEnglish
Japanese
Published The Japanese Society of Nutrition and Dietetics 30.05.1959
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Summary:In this report, characterization of protein of myosin fraction of clam muscle was studied with paper-electrophoresis. Paper-electrophoresis was conducted at ionic strength 0.1, 0.25 and 0.35, and at pH 7.2-7.5, about myosin A and myosin B fractions of adductor muscle of clam extracted with Weber-Edsall solution. From these experiments were resulted Fig. 1-3 and Table 1 as paper-electrophoretic diagrams having specialities. Particularly, in case of myosin A (Fig. 1, b) two peaks near the starting origin are remarkable, which are considered to be actomyosin and myosin or tropomyocin respectively.
ISSN:0021-5147
1883-7921
DOI:10.5264/eiyogakuzashi.17.107