Human somatotropin: semisynthesis of the hormone by noncovalent interaction of the natural NH2-terminal fragment with a synthetic analog of the COOH-terminal fragment |
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Authors: | C H Li J Blake C H Cheng M D Jibson |
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Affiliation: | Hormone Research Laboratory, University of California, San Francisco, California 94143 USA |
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Abstract: | Complementation of the natural [Cys (Cam)53]-HGH-(1–134) fragment with synthetic analogs of COOH-terminal fragments of human somatotropin (HGH), namely [Nle170, Ala165,182]-HGH-(140–182) and [Nle170,Ala165,182]-HGH-(140–187) has been investigated. It was found that the synthetic fragment, [Nle170,Ala165,182]-HGH-(140–187), gave a recombinant with about 40% HGH radioreceptor-binding activity. When compared with the natural recombinant, the semisynthetic hormone exhibited similar receptor-binding activities. The natural and semisynthetic recombinants were indistinguishable in radioimmunoassay. The α-helical content of the semisynthetic recombinant was completely restored in comparison with that of the native hormone as revealed by circular dichroism spectra. On the other hand, attempts to obtain a recombinant with the synthetic [Nle170,Ala165,182]-HGH-(140–182) were unsuccessful. The synthesis of [Nle170,Ala165,182]-HGH-(140–182) and [Nle170,Ala165,182]-HGH-(140–187) is herein described. |
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