Amino acid sequence around the active site cysteine residue of calcium-activated neutral protease (CANP) |
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Authors: | K Suzuki H Hayashi T Hayashi K Iwai |
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Affiliation: | Laboratoire de Physiologie Végétale, Université de Neuchâtel, Chantemerle 20, CH-2000 Neuchâtel, Switzerland |
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Abstract: | We have examined hydrophobic properties of Tetrahymena CaM using the uncharged probe, n-phenyl-1-naphthylamine (NPN) fluorescence. The maximal fluorescence intensity of Tetrahymena calmodulin (CaM) is less than 1/12 of that of the bovine brain CaM. In the phosphodiesterase activation, the potency of Tetrahymena CaM, which was represented by reciprocals of the quantity of CaM required for half-maximal activation of enzyme was 22.7% respectively, of that of the bovine brain CaM. Here, Tetrahymena CaM had less hydrophobic groups exposed in the presence of Ca2+. Then Ca2+-CaM dependent enzymes require much amount of Tetrahymena CaM, comparing with the bovine brain CaM. |
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Keywords: | ATPase Chloroplast envelope Spinach Calmodulin Cation activation |
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