Proceedings of the National Academy of Sciences · 1976 · 69 citations · 17 references
Life SciencesBiochemistryMolecular BiologyHormone BiochemistryProtein EngineeringProtein FoldingGrowth HormoneGrowth Hormone RegulationHormone Binding ProteinsHormone InactivationHormone StructurePituitary HormonesBiological Activity FeaturesCircular DichroismCircular Dichroism AnalysisGrowth Hormone StructurePh DependencePituitary Hormone BiochemistryPituitary Peptide HormonesRecombinant Human Growth Hormone
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 completely repaired in comparison with that of the native hormone.
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BIOASSAY OF HYPOPHYSEAL GROWTH HORMONE: THE TIBIA TEST<sup>1</sup>
Francis S. Greenspan, Choh Hao Li, Miriam E. Simpson et al. · Endocrinology · 1949 · 370 citations