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Perturbed angular correlation studies of the metal-binding sites in ovotransferrin and its C- and N-terminal halves

✍ Scribed by F. J. Schwab; H. Appel; A. B. Mason; M. Neu; W.-G. Thies


Publisher
Springer Netherlands
Year
1993
Tongue
English
Weight
771 KB
Volume
6
Category
Article
ISSN
1572-8773

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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 (M r 32 549), which inhibited tropomyosin-enhanced actomyosin Mg2+-ATPase activity by 90