Skyler J S, Chrambach A, Li C H
Biochim Biophys Acta. 1977 Apr 25;491(2):566-72. doi: 10.1016/0005-2795(77)90302-6.
A preparation of human pituitary somatotropin examined in quantitative polyacrylamide gel electrophoresis is conformationally compact. The derived molecular weight by quantitative electrophoresis is consistant with the known mass of the hormone and value obtained by other methods. A plasmin-modified somatotropin is more compact and shows full activity in immunoassay, and in lymphocyte binding and somatotropic assays, with enhanced lactogenic activity. The N-terminal 134-amino acid fragment and a hendekakaihekaton fragment exist in non-monomeric forms. The N-terminal fragment has immunologic and biologic activity, with greatest activity in the in vivo somatotropic assay. The hendekakaihekaton fragment exhibited only marginal activity. All preparations showed heterogeneity of charge in quantitative electrophoresis with discreet charge isomerism recognizable for the native and plasmin-modified preparations.
在定量聚丙烯酰胺凝胶电泳中检测的人垂体生长激素制剂构象紧密。通过定量电泳得出的分子量与该激素的已知质量以及通过其他方法获得的值一致。纤溶酶修饰的生长激素更紧密，在免疫测定、淋巴细胞结合和生长激素测定中显示出完全活性，且催乳活性增强。N端134个氨基酸片段和一个126肽片段以非单体形式存在。N端片段具有免疫和生物活性，在体内生长激素测定中活性最高。126肽片段仅表现出微弱活性。所有制剂在定量电泳中均显示电荷异质性，天然和纤溶酶修饰的制剂均可识别出离散的电荷异构现象。
