The primary structure of a new Mr 18,000 calcium vector protein from amphioxus.
作者： T. Kobayashi , T. Takagi , K. Konishi , J.A. Cox
DOI: 10.1016/S0021-9258(18)61550-9
关键词:
摘要: The amino acid sequence of a new Ca2+-binding protein (CaVP) from Amphioxus muscle (Cox, J. A., Biol. Chem. 261, 13173-13178) has been determined. contains 161 residues and molecular weight 18,267. N terminus is blocked by an acetyl group. two functional sites have localized based on homology with known domains, internal secondary structure prediction, appear to be the domains III IV. C-terminal half CaVP, which sites, shows remarkable similarity human brain calmodulin (45%) rabbit skeletal troponin C (40%). Functional domain 2 epsilon-N-trimethyllysine in alpha-helices flanking loop. Sequence determination revealed abortive N-terminal CaVP 24 30% as compared C, respectively. This also characterized presence disulfide bridge linking helix I II. bond very resistant reduction native state, but not denatured CaVP. optically interesting aromatic chromophores (2 tryptophan 1 tyrosine residues) are all located nonfunctional
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