Key result
Polyclonal caldesmon antibodies cross-reacting with rabbit skeletal troponin T compete with smooth muscle tropomyosin for caldesmon and troponin T in vitro.
Provides functional confirmation that regions of amino acid sequence homology in caldesmon isoforms and troponin T belong to tropomyosin binding sites.
Confirms functional homology at tropomyosin-binding sites in vitro; leaves open relevance to in vivo contractility or human disease.
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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Birukov et al. (1990) studied this question. Polyclonal caldesmon antibodies was evaluated on Competitive binding to caldesmon and troponin T. Polyclonal caldesmon antibodies cross-reacting with rabbit skeletal troponin T compete with smooth muscle tropomyosin for caldesmon and troponin T in vitro.
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