Solubilization of membrane-bound adenylate cyclase of isolated rat adrenal cortex cells |
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Authors: | Marianne Pilaski Klaus-Dieter Voigt Wolfgang Walter |
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Affiliation: | 1. Department of Clinical Chemistry, University Hospital, 2000 Hamburg, F.R.G.;2. Institute of Organic Chemistry, University of Hamburg, 2000 Hamburg, F.R.G. |
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Abstract: | The membrane-bound adenylate cyclase (ATP pyrophosphate-lyase (cyclizing), EC 4.6.1.1) of isolated rat adrenal cortex cells can be rendered soluble using 0.02 M Lubrol 12A9. The solubilized enzyme can be filtered through Millipore filters with pores 0.22 μm in diameter. Using gel filtration, on Sephadex G-200, adenylate cyclase activity was eluted with a distribution coefficient of 0.139, whereas on Sephadex G-100 the activity was eluted in the excluded volume. Half-maximum activation of the postulated guanyl nucleotide regulator site of adenylate was achieved with 5′-guanylyl-imidodiphosphate at a concentration of 1 · 10?6 M. In contrast, however, using intact isolated rat adrenal cortex cells the guanyl nucleotide regulator site could not be stimulated by 5′-guanylyl-imidodiphosphate. |
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Keywords: | Adenylate cyclase 5′-Guanylyl-imidodiphosphate (Adrenal cortex) |
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