Biochemical and Immunochemical Analysis of Avianβ₁ and Mammalian β₂-Adrenergic Receptors

M. P. Chapot Departmentof Biotechnology, Pasteur Institute and University, Paris VII 25, rue du Docteur Roux, 75015, PARIS, France

P. Cervantes Departmentof Biotechnology, Pasteur Institute and University, Paris VII 25, rue du Docteur Roux, 75015, PARIS, France

S. Kaveri Departmentof Biotechnology, Pasteur Institute and University, Paris VII 25, rue du Docteur Roux, 75015, PARIS, France

O. Durieu-Trautmann Departmentof Biotechnology, Pasteur Institute and University, Paris VII 25, rue du Docteur Roux, 75015, PARIS, France

C. Delavier-Klutchko Departmentof Biotechnology, Pasteur Institute and University, Paris VII 25, rue du Docteur Roux, 75015, PARIS, France

L. Emorine Departmentof Biotechnology, Pasteur Institute and University, Paris VII 25, rue du Docteur Roux, 75015, PARIS, France

P. O. Couraud Departmentof Biotechnology, Pasteur Institute and University, Paris VII 25, rue du Docteur Roux, 75015, PARIS, France

A. D. Strosberg Departmentof Biotechnology, Pasteur Institute and University, Paris VII 25, rue du Docteur Roux, 75015, PARIS, France

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Abstract

We have studied the molecular properties of avian β₁-adrenergic receptor and human β₂-adrenergic receptor.

The turkey erythrocytes β₁-receptor has been solubilized in active form by digitonin and has been purified to homogeneity by affinity chromatography followed by electroelution from polyacrylamide gel.

The photoactivable ligand, iodocyanopindololdiazirine, labels specifically a major 45 kDa and minor 55 kDa polypeptide in turkey erythrocytes, whereas in A431, it labels two polypeptides of molecular weights 65 kDa and 55 kDa.

Both types of receptors are N- and possibly O-glycosylated but the turkey β₁ receptor has only complex carbohydrates whereas the human β₂ receptor has in addition oligo mannosidic polysaccharidic moiety.

Polyclonal and monoclonal antibodies were raised against the β₁- and β₂-adrenergic receptors.

Polyclonal antibodies were found to mimic β-adrenergic agonists by stimulating adenylate cyclase upon binding to the receptors. The monoclonal antibodies precipitated both intact and affinity labeled receptors which they also revealed on immunoblots.

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Biochemical and Immunochemical Analysis of Avianβ₁ and Mammalian β₂-Adrenergic Receptors

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Biochemical and Immunochemical Analysis of Avianβ₁ and Mammalian β₂-Adrenergic Receptors