Sequence analysis of somatomedin-C: confirmation of identity with insulin-like growth factor I.
Sequence analysis of somatomedin-C: confirmation of identity with insulin-like growth factor I.
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DOI：
10.1210/endo-112-6-2215
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发表时间：
1983-06
期刊：
影响因子：
4.8
通讯作者：
D. Klapper;M. Svoboda;J. J. Wyk-J.
中科院分区：
文献类型：
--
作者：
D. Klapper;M. Svoboda;J. J. Wyk-J.
生长调节素-C（Sm-C）是通过先前公布的方法从人血浆的Cohn组分IV中纯化的。通过SDS聚丙烯酰胺电泳，然后对凝胶进行银染色确定纯度。酸水解产物的氨基酸分析显示与胰岛素样生长因子I（IGF-I）的氨基酸组成没有显着差异。从氨基末端甘氨酸开始的前24个残基与IGF-I中的相应残基相同。胰蛋白酶和胰凝乳蛋白酶降解，然后测定所得肽的氨基酸组成和序列，以完成Sm-C的一级结构。这些研究的结果证明Sm-C和IGF-I是相同的肽，从而支持先前的观察结果，即Sm-C和IGF-I在放射性配体和生物测定系统中定性和定量无法区分。
Somatomedin-C (Sm-C) was purified from Cohn fraction IV of human plasma by previously published methods. Purity was established by SDS polyacrylamide electrophoresis followed by silver staining of the gel. Amino acid analysis of an acid hydrolysate revealed no significant discrepancies from the amino acid composition of insulin-like growth factor I (IGF-I). The first 24 residues beginning at the amino terminal glycine were identical to the corresponding residues in IGF-I. Tryptic and chymotryptic degradation followed by determination of the amino acid composition and sequence of the resultant peptides was used to complete the primary structure of Sm-C. The results of these studies document that Sm-C and IGF-I are identical peptides, thus supporting previous observations that Sm-C and IGF-I are qualitatively and quantitatively indistinguishable in radioligand and biological assay systems.