The cloning and sequence analysis of Chinese human cardiac myosin light chain 1 (CCMLC1) was previously reported. In this paper the cDNA of CCMLC1 was used as template and both of cDNAs of N and C terminal fragments of CCMLC1, each containing 98 amino acid residues, were obtained by PCR. Using the expressed products of both fragments, the binding experiments of two fragments to cardiacmyosin heavy chain of rat, human cardiac actin and to monoclonal antibody raised against CCMLC1, have been performed, respectively, by means of precipitation with GST-Sepharose beads. The results showed that all the heavy chain, actin and monoclonal antibody bound the N terminal fragment of CCMLC1 at different sites. Under experimental conditions, the binding of CCMLC1 with actin could affect the subsequent binding of CCMLC1 to heavy chain in topologically.
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