Noncovalent interaction of the NH2-terminal fragment of human somatotropin with the COOH-terminal fragment of human choriomammotropin to generate growth-promoting activity.

C H Li

doi:10.1073/pnas.75.4.1700

Noncovalent interaction of the NH2-terminal fragment of human somatotropin with the COOH-terminal fragment of human choriomammotropin to generate growth-promoting activity.

C H Li

Open Access

https://doi.org/10.1073/pnas.75.4.1700

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Journal: Proceedings of the National Academy of Sciences	Publication Date: Apr 1, 1978
Citations: 15

#Growth-promoting Activity #Human Somatotropin + Show 8 more

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Abstract

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.

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