Schleyer M, Mayer C
Proteinlabor der Abteilung Innere Medizin I, Universität Ulm.
Biol Chem Hoppe Seyler. 1990 Oct;371(10):1009-14. doi: 10.1515/bchm3.1990.371.2.1009.
In polyacrylamide gel electrophoresis and isoelectric focusing, somatotropin produced by recombinant DNA technology is as heterogeneous as highly purified native pituitary somatotropin. This heterogeneity is not attributable to different degrees of deamination of a single molecular species. In addition to the main protein of 22 kDa, the cloned products contain traces of interchain disulphide dimers of somatotropin. The quantitative amino acid analyses of the three cloned somatotropins investigated are neither identical nor do they correspond to the analysis of the native pituitary hormone. Moreover, there are discrepancies between the amino acid compositions of the hormones studied and the generally recognized amino acid analysis for human somatotropin.
在聚丙烯酰胺凝胶电泳和等电聚焦中，通过重组DNA技术生产的生长激素与高度纯化的天然垂体生长激素一样具有异质性。这种异质性并非归因于单一分子物种不同程度的脱氨基作用。除了22 kDa的主要蛋白质外，克隆产物还含有痕量的生长激素链间二硫键二聚体。所研究的三种克隆生长激素的定量氨基酸分析既不相同，也与天然垂体激素的分析结果不符。此外，所研究激素的氨基酸组成与普遍认可的人生长激素氨基酸分析结果之间存在差异。
