Octopus calmodulin. Structural comparison with bovine brain calmodulin.
نویسندگان
چکیده
منابع مشابه
Calmodulin and calmodulin-binding proteins in brain.
filament preparations isolated from many different species. Incubation of crude and purified preparations of filaments with [f2P]ATP labels nearly all the filament proteins (Fig. l), the exception being the 65000-mol.wt. band of Loligo (Fig. la). Phosphorylation in vitro is mediated by a cyclic AMPand Ca2+-independent, and Mg2+-dependent, protein kinase. The enzyme is activated by Na+ and K+ an...
متن کاملDemonstration and purification of multiple bovine brain and bovine lung calmodulin-stimulated phosphatase isozymes.
Calmodulin (CaM)-stimulated phosphatase in bovine brain or bovine lung CaM-binding protein fractions were fractionated on a heparin-Sepharose column into three activity peaks, designated in order of column three activity peaks, designated in order of column elution as the brain peak I (BPI), peak II (BPII), and peak III (BPIII) or the lung peak I (LPI), peak II (LPII), and peak III (LPIII) phos...
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A rabbit lung cyclic nucleotide phosphodiesterase (PDE) prepared by successive chromatography on DEAE-cellulose and G-200 Sephadex columns in the presence of EGTA was activated by Ca2+ and contained calmodulin (CaM), suggesting that the enzyme exists as a stable CaM.PDE complex (Sharma, R. K., and Wirch, E. (1979) Biochem. Biophys. Res. Commun. 91,338-344). An enzyme with similar properties ...
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Objective(s): The rotavirus nonstructural protein 4 (NSP4) is responsible for the increase in cytoplasmic calcium concentration through a phospholipase C-dependent and phospholipase C-independent pathways in infected cells. It is shown that increasing of intracellular calcium concentration in rotavirus infected cells is associated with the activation of some members of protein kinases family su...
متن کاملUnbiased simulation of structural transitions in calmodulin
We introduce an approach for performing “very long” computer simulations of the dynamics of simplified, folded proteins. Using an alpha-carbon protein model and a fine grid to mimic continuum computations at increased speed, we perform unbiased simulations which exhibit many large-scale conformational transitions at low cost. In the case of the 72-residue N-terminal domain of calmodulin, the ap...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1980
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)70178-1