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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1978 Apr;75(4):1700–1702. 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
PMCID: PMC392406  PMID: 273900

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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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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