Purification and characterization of an algal (Dunaliella tertiolecta) protein cross-reacting with an anti-Ga-common antibody |
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| Authors: | Koji Takahashi Takashi Yuasa Shoshi Muto |
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| Institution: | K. Takahashi, Graduate School of Agricultural Sciences, Nagoya Univ., Chikusa-ku. Nagoya. 464–01, Japan: T. Yuasa and S. Muto (corresponding author), Nagoya Univ. BioScience Center, Nagoya Univ., Chikusa-ku, Nagoya, 464–01. Japan |
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| Abstract: | A 26-kDa and a 36-kDa protein that cross-reacted with anti-Ga-common and anti-Gβ antibodies, respectively, were detected in Dunaliella cells. The 26-kDa protein was solubilized from a crude membrane fraction with deoxycholate and purified to homogeneity by DE52 and hydroxylapatite chromatography and DEAE-5PW high performance liquid chromatography (HPLC). The hydroxylapatite-purified preparation had GTPγS binding and GTPase activities, but the homogeneous 26-kDa protein had none. The sequence of the 28 N-terminal amino acids of the 26-kDa protein had no homology to any GTP binding protein thus far reported. |
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| Keywords: | Gα Gβ GTP binding protein Dunaliella tertiolecta |
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