By Professor Dr. med. Alexis Labhart (auth.)
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Example text
The soluble receptor turned out to be a protein, as had been predicted on the basis of the more indirect studies. Lipids are probably not an essential part in the function of this receptor. The estimated molecular weight was 300000. Proteins seem particularly suited to the task of receptors since they are capable of binding a great variety of substances ranging from simple ions to large macromolecules. This property of proteins was extensively analyzed by SCATCHARD as early as 1949. MONOD (1966) discussed the possibility that hormones might be allosteric ligands, and hormone receptors allosteric proteins.
2a. Enzymatic degradation of cyclic AMP. 3. Cyclic AMP binds to a regulatory subunit of the protein kinase. This leads to dissociation of the regulatory subunit from the catalytic subunit, the latter becoming active. 4. Phosphorylation of the inactive phosphorylase kinase. 5. Phosphorylation of the inactive phosphorylase. 6. Removal of glucose-1-phosphate from glycogen by phosphorolysis. Abbreviations: ATP: Adenosine triphosphate; ADP (AMP): Adenosine-di-(mono) phosphate; GTP: Guanosine triphosphate; Pi: Inorganic phosphate 12 Cyclic AMP is produced from adenosine triphosphate (ATP) through the enzyme adenyl cyclase.
Both observations strongly implicate hydrophobic interactions between hormone and receptor. In the case of protein and peptide hormones which contain disulfide bridges (insulin, antidiuretic hormone), the possibility has been considered that covalent bonds may occur with sulfhydryl groups of the receptors through the formation of a mixed disulfide between receptor and hormone. The in-vitro action of insulin upon adipose or muscle tissue can in fact be prevented by the use of sulfhydrylblocking agents such as N-ethyl maleimide (OTT, 1963).