Noncovalent interaction of the NH2-terminal fragment of human somatotropin with the COOH-terminal fragment of human choriomammotropin to generate growth-promoting activity.
نویسنده
چکیده
Complementation of the plasmin fragments of reduced-carbamoylmethylated (Cam) human somatotropin (hGH) with those of reduced-carbamoylmethylated human chorionic somatomammotropin (hCS) have been investigated. It was found that the recombinant obtained by noncovalent interaction of [Cys(Cam)53]hGH-(1-134) with [Cys(Cam)-165,182,189]hCS-(141-191) exhibits 50% growth-promoting activity and nearly full immunoreactivity. Complementation of [Cys(Cam)53]hCS-(1-133) with the COOH-terminal fragment of hGH generated lower growth-promoting and immunological activities.
منابع مشابه
Human somatotropin: biological characterization of the recombinant molecule.
The recombinant hormone obtained by non-covalent interaction of the NH2-terminal 134 amino acid fragment with the COOH-terminal 51 amino acid fragment of the reduced-carbamidomethylated human somatotropin molecule is found to exhibit nearly full biological activity of the native hormone, as evidenced by the stimulation of hepatic ornithine decarboxylase (L-ornithine carboxy-lyase, EC 4.1.1.17) ...
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The NH2-terminal 134 amino-acid fragment of the reduced-carbamidomethylated human somatropin molecule is found to react noncovalently with the COOH-terminal 51 amino-acid fragment in solutions of pH 8.4 at 2 degrees to restore full biological activity as evidenced by the rat tibia and pigeon crop-sac assays. In addition, circular dichroism spectra of the recombinant show the conformation to be ...
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ورودعنوان ژورنال:
- Proceedings of the National Academy of Sciences of the United States of America
دوره 75 4 شماره
صفحات -
تاریخ انتشار 1978