Nagornaia L V, Kizim E A, Kravtsov G M, Tsibezov V V, Vinogradov V A
Biokhimiia. 1986 Aug;51(8):1348-54.
A combination of gel chromatography, fluorimetric analysis and polyacrylamide gel electrophoresis with immunochemical identification, the protein-peptide composition of secretory granules of the lactogenic hormone (LTH) isolated from the anterior lobe of bovine hypophysis was investigated. It was found that the peptide content of the granules is less than 3% of that of immunoreactive LTH. Using gel chromatography, the secretory granules were found to contain a hormone monomer and two immunoreactive forms with Mr 42 and 64 kD. With respect to immunoreactivity, the hormone form content was 90, 3 and 7%, respectively. Using polyacrylamide gel electrophoresis and subsequent immunochemical identification, the presence of four immunoreactive forms of LTH were identified in the secretory granules.
采用凝胶色谱法、荧光分析以及免疫化学鉴定的聚丙烯酰胺凝胶电泳相结合的方法，对从牛垂体前叶分离出的催乳激素（LTH）分泌颗粒的蛋白质 - 肽组成进行了研究。结果发现，颗粒中的肽含量不到免疫反应性LTH的3%。通过凝胶色谱法发现，分泌颗粒含有一种激素单体以及两种分子量分别为42kD和64kD的免疫反应形式。就免疫反应性而言，激素形式的含量分别为90%、3%和7%。利用聚丙烯酰胺凝胶电泳及随后的免疫化学鉴定，在分泌颗粒中鉴定出了四种LTH的免疫反应形式。
