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The regulatory proteins of the myofibril. Characterization and properties of the inhibitory factor (troponin B).

ABSTRACT: 1. Gel-filtration results indicate that the major component of inhibitory-factor preparations isolated by dissociation of the troponin complex consisted of a protein of subunit weight 23000 daltons. By the same procedure a molecular weight of 18000 was obtained for the calcium-sensitizing factor. 2. The inhibitory factor is specific for the actomyosin type of ATPase and ITPase. It is effective on desensitized actomyosin, natural actomyosin and intact myofibrils. 3. For inhibition, the actomyosin ATPase must be stimulated by Mg(2+), Ca(2+) or Mn(2+). The Co(2+)-, Cd(2+)- or Zn(2+)-stimulated ATPases are not affected. 4. Biological activity is stable to treatment with dissociating agents, heat, pH11, pH1 and carboxymethylation. 5. Increasing amounts of actin, but not myosin or tropomyosin, progressively neutralize the inhibitory activity when added to desensitized actomyosin or myofibrils.

SUBMITTER: Schaub MC

PROVIDER: S-EPMC1176967 | biostudies-other | 1971 Jul

REPOSITORIES: biostudies-other

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The regulatory proteins of the myofibril. Characterization and biological activity of the calcium-sensitizing factor (troponin A).

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