The Allosteric Inhibition by Calcium of Soluble and Partially Purified Adenylate Cyclase from Turkey Erythrocytes

Emmanuel HANSKI; Nehama SEVILLA; Alexander LEVITZKI

doi:10.1111/j.1432-1033.1977.tb11621.x

The Allosteric Inhibition by Calcium of Soluble and Partially Purified Adenylate Cyclase from Turkey Erythrocytes

Emmanuel HANSKI, Nehama SEVILLA, Alexander LEVITZKI^*

^*Corresponding author for this work

Institute for Medical Research Israel-Canada (IMRIC)

Research output: Contribution to journal › Article › peer-review

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Abstract

Adenylate cyclase from turkey erythrocyte membranes was solubilized in Lubrol‐PX and partially purified (22‐fold) by molecular sieve chromatography on Biogel A5M. The molecular weight of the enzyme was found to be 316000. The partially purified solubilized enzyme was found to retain all the kinetic and regulatory properties of the native membrane‐bound enzyme except its sensitivity to β‐agonists. The enzyme responds to Mg²⁺ in a positively cooperative fashion, with a Hill coefficient of n_H= 2.0. The enzyme is inhibited by Ca²⁺ in a positively cooperative fashion with a Hill coefficient of n_H= 2.0. The calcium effect is only on the K_cat of the reaction and not on the binding and kinetic parameters of the enzyme towards the other ligands such as MgATP and Mg²⁺. The Mn²⁺‐supported adenylate cyclase is not inhibited by Ca²⁺ as was found for the native membrane‐bound enzyme.

Original language	English
Pages (from-to)	513-520
Number of pages	8
Journal	European Journal of Biochemistry
Volume	76
Issue number	2
DOIs	https://doi.org/10.1111/j.1432-1033.1977.tb11621.x
State	Published - Jun 1977

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title = "The Allosteric Inhibition by Calcium of Soluble and Partially Purified Adenylate Cyclase from Turkey Erythrocytes",

abstract = "Adenylate cyclase from turkey erythrocyte membranes was solubilized in Lubrol‐PX and partially purified (22‐fold) by molecular sieve chromatography on Biogel A5M. The molecular weight of the enzyme was found to be 316000. The partially purified solubilized enzyme was found to retain all the kinetic and regulatory properties of the native membrane‐bound enzyme except its sensitivity to β‐agonists. The enzyme responds to Mg2+ in a positively cooperative fashion, with a Hill coefficient of nH= 2.0. The enzyme is inhibited by Ca2+ in a positively cooperative fashion with a Hill coefficient of nH= 2.0. The calcium effect is only on the Kcat of the reaction and not on the binding and kinetic parameters of the enzyme towards the other ligands such as MgATP and Mg2+. The Mn2+‐supported adenylate cyclase is not inhibited by Ca2+ as was found for the native membrane‐bound enzyme.",

author = "Emmanuel HANSKI and Nehama SEVILLA and Alexander LEVITZKI",

year = "1977",

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AU - LEVITZKI, Alexander

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N2 - Adenylate cyclase from turkey erythrocyte membranes was solubilized in Lubrol‐PX and partially purified (22‐fold) by molecular sieve chromatography on Biogel A5M. The molecular weight of the enzyme was found to be 316000. The partially purified solubilized enzyme was found to retain all the kinetic and regulatory properties of the native membrane‐bound enzyme except its sensitivity to β‐agonists. The enzyme responds to Mg2+ in a positively cooperative fashion, with a Hill coefficient of nH= 2.0. The enzyme is inhibited by Ca2+ in a positively cooperative fashion with a Hill coefficient of nH= 2.0. The calcium effect is only on the Kcat of the reaction and not on the binding and kinetic parameters of the enzyme towards the other ligands such as MgATP and Mg2+. The Mn2+‐supported adenylate cyclase is not inhibited by Ca2+ as was found for the native membrane‐bound enzyme.

AB - Adenylate cyclase from turkey erythrocyte membranes was solubilized in Lubrol‐PX and partially purified (22‐fold) by molecular sieve chromatography on Biogel A5M. The molecular weight of the enzyme was found to be 316000. The partially purified solubilized enzyme was found to retain all the kinetic and regulatory properties of the native membrane‐bound enzyme except its sensitivity to β‐agonists. The enzyme responds to Mg2+ in a positively cooperative fashion, with a Hill coefficient of nH= 2.0. The enzyme is inhibited by Ca2+ in a positively cooperative fashion with a Hill coefficient of nH= 2.0. The calcium effect is only on the Kcat of the reaction and not on the binding and kinetic parameters of the enzyme towards the other ligands such as MgATP and Mg2+. The Mn2+‐supported adenylate cyclase is not inhibited by Ca2+ as was found for the native membrane‐bound enzyme.

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The Allosteric Inhibition by Calcium of Soluble and Partially Purified Adenylate Cyclase from Turkey Erythrocytes

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