人生长激素：通过激素的天然片段与合成片段的非共价相互作用恢复完全生物活性。
Human somatotropin: restoration of full biological activity by noncovalent interaction of a natural and a synthetic fragment of the hormone.
作者信息
Li C H, Bewley T A, Blake J, Hayashida T
出版信息
Proc Natl Acad Sci U S A. 1977 Mar;74(3):1016-9. doi: 10.1073/pnas.74.3.1016.
Abstract
The recombinant hormone obtained by noncovalent interaction of the natural NH2-terminal fragment (consisting of 134 amino acid residues) with a synthetic COOH-terminal fragment of 52 amino acids of the reduced-carbamidomethylated human somatotropin molecule is found to exhibit full biological activity of the native hormone as evidenced by the tibia test. Radioimmunoassay data indicate that the semisynthetic recombinant hormone possesses essentially full immunoreactivity as compared to the native one. In addition, circular dichroism and fluorescence emission spectra of the semisynthetic recombinant are identical to that of the undisociated, plasmin modified, reduced-carbamidomethylated hormone.
摘要
通过天然NH2末端片段（由134个氨基酸残基组成）与还原氨甲酰甲基化人生长激素分子的52个氨基酸的合成COOH末端片段的非共价相互作用获得的重组激素，经胫骨试验证明具有天然激素的完全生物活性。放射免疫测定数据表明，与天然激素相比，半合成重组激素具有基本完全的免疫反应性。此外，半合成重组体的圆二色性和荧光发射光谱与未解离的、纤溶酶修饰的、还原氨甲酰甲基化激素的光谱相同。
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Comparative studies of the single tryptophan residue in human chorionic somatomammotropin and human pituitary growth hormone.人绒毛膜生长催乳素和人垂体生长激素中单个色氨酸残基的比较研究。
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