Identification of functioning regulatory sites and a new myosin binding site in the C-terminal 288 amino acids of caldesmon expressed from a human clone


A partial clone of caldesmon, coding for the C-terminal 288 amino acids, was isolated from a human fetal liver cDNA library and sequenced. Expression of the clone in Escherichia coli produced a peptide called H1 (Mr 32 549), which inhibited tropomyosin-enhanced actomyosin Mg2+-ATPase activity by 90% with half maximal inhibition at 0.03–0.04 mol H1 per mol… (More)
DOI: 10.1007/BF00121289


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