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Spectroscopic evidence of two melittin molecules bound to Ca2+-calmodulin.

作者信息

Follenius-Wund A, Mely Y, Gerard D

机构信息

Laboratoire de Physique, U.A. 491 CNRS, Université Louis Pasteur, Faculte de Pharmacie, Strasbourg, France.

出版信息

Biochem Int. 1987 Oct;15(4):823-33.

PMID:3435546
Abstract

According to Comte et al. (Comte, M., Maulet, Y. and Cox, J.A., (1983), Biochem.J., 209, 269-272), melittin (Mel) gives rise to a one:one complex. We evidence here, by fluorescence anisotropy and gel filtration binding assay (in the presence of 5 mM CaCl2 and 100 mM NaCl) the existence of two complexes: the well-known CaM.Ca4.Mel and a second CaM.Ca4.Mel2 which had not yet been reported. The affinity of Mel for the CaM.Ca4.Mel species is about three orders of magnitude lower than the affinity of Mel for the CaM-Ca4 species.

摘要

相似文献

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Spectroscopic evidence of two melittin molecules bound to Ca2+-calmodulin.
Biochem Int. 1987 Oct;15(4):823-33.
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引用本文的文献

1
Distribution of distances between the tryptophan and the N-terminal residue of melittin in its complex with calmodulin, troponin C, and phospholipids.蜂毒肽与钙调蛋白、肌钙蛋白C及磷脂形成的复合物中,色氨酸与蜂毒肽N端残基之间的距离分布。
Protein Sci. 1994 Apr;3(4):628-37. doi: 10.1002/pro.5560030411.