Glycosylated human growth hormone (hGH): a novel 24 kDa hGH-N variant.
Glycosylated human growth hormone (hGH): a novel 24 kDa hGH-N variant.
复制标题
糖基化人生长激素 (hGH)：一种新型 24 kDa hGH-N 变体。
DOI：
10.1006/bbrc.1996.1697
复制
发表时间：
1996
期刊：
影响因子：
--
通讯作者：
Ling,NC
中科院分区：
文献类型：
--
作者：
Haro,LS;Lewis,UJ;Garcia,M;Bustamante,J;Martinez,AO;Ling,NC
我们发现了一种新的hGH糖基化变异体，即人类脑下垂体蛋白。变性蛋白的分离包括用Sephadex G-100碳酸氢铵柱层析，然后用10%冰醋酸Sephadex G-100柱层析，再用碳酸氢铵DEAE Sephacryl柱层析，最后用制备性的SDS PAGE。经SDS-PAGE分析，该蛋白的相对分子质量为24 kDa，大于正常的22 kDa hGH。对前26个残基的N-末端氨基酸序列分析表明，该蛋白不是hGH-V基因产物，而是hGH-N基因产物。糖偶联物的检测(高碘酸氧化、唾液酸酶处理、三氟甲磺酸处理)表明，hGH变异体含有碳水化合物部分。新的hGH的发现提出了关于糖基化在这种激素的结构/功能关系中的作用的问题。
We have identified a human pituitary protein as a novel glycosylated variant of hGH. Isolation of the denatured protein included separation of human pituitary extract by Sephadex G-100 chromatography in ammonium bicarbonate, followed by Sephadex G-100 chromatography in 10% acetic acid, with subsequent DEAE Sephacryl chromatography in ammonium bicarbonate, and finally by preparative SDS PAGE. The pituitary protein has a molecular weight of 24 kDa as determined by SDS PAGE analysis and is thus larger than the normal 22 kDa hGH. N-Terminal amino acid sequence analysis of the first twenty-six residues reveals that this protein is not derived from the hGH-V gene but is rather a hGH-N gene product. Assays for the detection of glycoconjugates (periodate oxidation, sialidase treatment, trifluoromethanesulfonic acid treatment) indicate that the hGH variant has carbohydrate moieties. The discovery of new hGH raises questions about the role of glycosylation in the structure/function relationships of this hormone.