垂体促卵泡素的研究。十二。化学去糖基化诱导的热稳定性增强。

Studies on pituitary follitropin. XII. Enhanced thermal stability induced by chemical deglycosylation.

作者信息

Sairam M R, Manjunath P

出版信息

Mol Cell Endocrinol. 1982 Oct;28(2):151-9. doi: 10.1016/0303-7207(82)90028-4.

Abstract

The receptor binding, immunological and biological activities of ovine follitropin were rapidly destroyed when aqueous solutions were kept in a boiling water bath. Similar treatment of the chemically deglycosylated follitropin (DG-FSH) showed less drastic effects on its hormonal properties. The latter preparation was more stable to heat treatment. A 30-min heat-treated DG-FSH was as active as native follitropin in the receptor-binding assay. Heat-treated DG-FSH solution still retained its capability to antagonize the action of native follitropin in the in vitro bioassay. The conformational features of deglycosylated follitropin required for receptor binding and immunological reactivity are preserved after heat treatment.

摘要

当将水溶液置于沸水浴中时，绵羊促卵泡素的受体结合、免疫及生物学活性会迅速遭到破坏。对化学去糖基化促卵泡素（DG - FSH）进行类似处理时，其激素特性受到的影响较小。后一种制剂对热处理更稳定。在受体结合试验中，经30分钟热处理的DG - FSH与天然促卵泡素活性相当。在体外生物测定中，经热处理的DG - FSH溶液仍保留拮抗天然促卵泡素作用的能力。热处理后，去糖基化促卵泡素受体结合及免疫反应所需的构象特征得以保留。