1990FEBS LettersRequires access

Competitive binding of the troponin T‐specific pool of caldesmon antibodies and tropomyosin to skeletal troponin T and smooth muscle caldesmon

Konstantin G. Birukov, Vladimir P. Shirinsky, Alexander V. Vorotnikov, Nikolai B. Gusev

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Abstract

The fraction of polyclonal caldesmon antibodies cross-reacting with rabbit skeletal troponin T are shown to compete with smooth muscle tropomyosin for caldesmon and troponin T, as revealed by ELISA method. The epitope recognized by these antibodies was also found in Mr 77 kDa non-muscle caldesmon. These results provide functional confirmation for the suggestion that the regions of amino acid sequence homology in caldesmon isoforms and troponin T belong to the tropomyosin binding sites.

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The fraction of polyclonal caldesmon antibodies cross-reacting with rabbit skeletal troponin T are shown to compete with smooth muscle tropomyosin for caldesmon and troponin T, as revealed by ELISA method. The epitope recognized by these antibodies was also found in Mr 77 kDa non-muscle caldesmon. These results provide functional confirmation for the suggestion that the regions of amino acid sequence homology in caldesmon isoforms and troponin T belong to the tropomyosin binding sites.

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Available abstract

The fraction of polyclonal caldesmon antibodies cross-reacting with rabbit skeletal troponin T are shown to compete with smooth muscle tropomyosin for caldesmon and troponin T, as revealed by ELISA method. The epitope recognized by these antibodies was also found in Mr 77 kDa non-muscle caldesmon. These results provide functional confirmation for the suggestion that the regions of amino acid sequence homology in caldesmon isoforms and troponin T belong to the tropomyosin binding sites.

Key concepts: Caldesmon, Tropomyosin, Polyclonal antibodies, Troponin T, Troponin C, Troponin, Epitope, Molecular biology

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Competitive binding of the troponin T‐specific pool of caldesmon antibodies and tropomyosin to skeletal troponin T and smooth muscle caldesmon — Research Paper | ScholarLens