Literature DB >> 6111560

Tetrahymena calcium-binding protein is indeed a calmodulin.

Y Suzuki, S Nagao, K Abe, T Hirabayashi, Y Watanabe.   

Abstract

We previously isolated a Ca2+-binding protein from a ciliate, Tetrahymena, and designated it as TCBP (Tetrahymena Ca2+-binding protein). The present paper reports that TCBP, which has two high affinity Ca2+-binding sites (Kd=4.6 X 10(-6) M), could activate porcine brain cyclic nucleotide phosphodiesterase at a concentration of over 10(-6) M free Ca2+, with the same mode of activation as that of authentic (porcine brain) calmodulin. In addition, the amino acid composition of TCBP was essentially the same as that of brain calmodulin. Therefore, we conclude that TCBP as an activator of Tetrahymena guanylate cyclase is indeed a calmodulin.

Entities:  

Mesh:

Substances:

Year:  1981        PMID: 6111560     DOI: 10.1093/oxfordjournals.jbchem.a133200

Source DB:  PubMed          Journal:  J Biochem        ISSN: 0021-924X            Impact factor:   3.387


  2 in total

1.  The two domains of centrin have distinct basal body functions in Tetrahymena.

Authors:  Tyson Vonderfecht; Alexander J Stemm-Wolf; Melissa Hendershott; Thomas H Giddings; Janet B Meehl; Mark Winey
Journal:  Mol Biol Cell       Date:  2011-05-11       Impact factor: 4.138

2.  Immune localization of calmodulin in the ciliated cells of hamster tracheal epithelium.

Authors:  R E Gordon; K B Williams; S Puszkin
Journal:  J Cell Biol       Date:  1982-10       Impact factor: 10.539

  2 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.