人生长激素：重组分子的生物学特性
Human somatotropin: biological characterization of the recombinant molecule.
作者信息
Li C H, Hayashida T, Doneen B A, Rao A J
出版信息
Proc Natl Acad Sci U S A. 1976 Oct;73(10):3463-5. doi: 10.1073/pnas.73.10.3463.
Abstract
The recombinant hormone obtained by non-covalent interaction of the NH2-terminal 134 amino acid fragment with the COOH-terminal 51 amino acid fragment of the reduced-carbamidomethylated human somatotropin molecule is found to exhibit nearly full biological activity of the native hormone, as evidenced by the stimulation of hepatic ornithine decarboxylase (L-ornithine carboxy-lyase, EC 4.1.1.17) in vivo and protein synthesis in mouse mammary gland in vitro. Radioimmunoassay data indicate that the recombinant behaves immunochemically in a manner almost identical to that of the native hormone.
摘要
通过还原氨甲酰甲基化人生长激素分子的NH2末端134个氨基酸片段与COOH末端51个氨基酸片段的非共价相互作用获得的重组激素，被发现具有近乎天然激素的全部生物活性，这在体内对肝鸟氨酸脱羧酶（L-鸟氨酸羧基裂解酶，EC 4.1.1.17）的刺激以及体外对小鼠乳腺蛋白质合成的刺激中得到了证明。放射免疫分析数据表明，该重组体在免疫化学行为上几乎与天然激素相同。
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