NDLI: Isolation of adenylate cyclase-free, beta-adrenergic receptor from turkey erythrocyte membranes by affinity chromatography.

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Isolation of adenylate cyclase-free, beta-adrenergic receptor from turkey erythrocyte membranes by affinity chromatography.

Reconstitution of catecholamine-sensitive adenylate cyclase activity: interactions of solubilized components with receptor-replete membranes.

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Variants of 3T3 cells lacking mitogenic response to epidermal growth factor.

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Mutator action by Escherichia coli strains carrying dnaE mutations.

Filamentous coliphage M13 as a cloning vehicle: insertion of a HindII fragment of the lac regulatory region in M13 replicative form in vitro.

Electron microscope studies of transient complexes formed between Escherichia coli RNA polymerase holoenzyme and T7 DNA.

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Isolation of adenylate cyclase-free, beta-adrenergic receptor from turkey erythrocyte membranes by affinity chromatography.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Hanoune, J. Strosberg, A. D. Geynet, P. Vauquelin, G.
Abstract	The adenylate cyclase [ATP pyrophosphatelyase (cyclizing); EC 4.6.1.1] and beta-adrenergic receptor of plasma membranes of turkey erythrocytes were solubilized in an active form by treatment with either NaF or guanylylimidodiphosphate and digitonin. The solubilized enzyme was no longer stimulated by catecholamines, NaF, or guanine nucleotides. The digitonin extract was chromatographed on an alprenolol-agarose derivative. While the bulk of protein and all the adenylate cyclase activity passed unretarded through the column, the receptor was retained. It eluted free of enzyme activity with an alprenolol solution containing 1 M NaCl; the yield was 25-30%. The protein content of the alprenolol eluates was too low to be estimated by the Lowry technique and was assessed by a more sensitive fluorometric method. Under these conditions, the beta-adrenergic receptor was purified approximately 2000-fold in a single step with retention of all its pharmacological properties. These experiments establish that the beta-adrenergic receptor and the adenylate cyclase are independent entities which may be separated on a functional basis.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	9
Volume Number	74
Language	English
Publisher	National Academy of Sciences
Publisher Date	1977-11-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Adenylate Cyclase Blood Erythrocyte Membrane Metabolism Erythrocytes Receptors, Adrenergic, Beta Receptors, Adrenergic Isolation & Purification Alprenolol Animals Binding, Competitive Chromatography, Affinity Kinetics Turkeys Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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