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The membrane-bound adenylase cyclase (ATP pyrosphosphate-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 Milipore filters with pores 0.22 micron 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.
M Pilaski, and
K D Voigt, and
W Walter
January 1975,
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M Pilaski, and
K D Voigt, and
W Walter
September 1982,
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M Pilaski, and
K D Voigt, and
W Walter
January 1974,
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M Pilaski, and
K D Voigt, and
W Walter
August 1980,
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M Pilaski, and
K D Voigt, and
W Walter
February 1979,
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M Pilaski, and
K D Voigt, and
W Walter
December 1980,
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M Pilaski, and
K D Voigt, and
W Walter
October 1977,
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M Pilaski, and
K D Voigt, and
W Walter
May 1973,
Biochemistry,
M Pilaski, and
K D Voigt, and
W Walter
July 1984,
Endocrinology,
M Pilaski, and
K D Voigt, and
W Walter
February 1973,
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