Campbell C J, Charlton P A, Grinham C J, Mooney C J, Pendlebury J E
Biochem J. 1987 Apr 1;243(1):121-6. doi: 10.1042/bj2430121.
Human angiotensinogen has been purified 390-fold from serum by a rapid high-yielding procedure that involved chromatography on Blue Sepharose, phenyl-Sepharose, hydroxyapatite and immobilized 5-hydroxytryptamine (5-HT). Angiotensinogen was specifically bound to immobilized 5-HT, which effected a partial resolution into multiple forms, which were also evident when analysed by SDS/polyacrylamide-gel electrophoresis (Mr 59,400, 60,600, 62,600 and 63,800). This heterogeneity was confirmed by resolution into six main bands on isoelectric focusing, ranging from pI 4.40 to 4.82. N-terminal analysis, digestion with human renal renin and deglycosylation studies implied that the preparation comprised several forms of angiotensinogen, varying in their degree of glycosylation. The presence of sialic acid was shown to be a major factor in determining the heterogeneity.
通过一种快速高产的方法，已从血清中纯化出390倍的人血管紧张素原，该方法包括在蓝色琼脂糖凝胶、苯基琼脂糖凝胶、羟基磷灰石和固定化5-羟色胺（5-HT）上进行色谱分离。血管紧张素原特异性结合到固定化的5-HT上，这导致部分分离为多种形式，通过SDS/聚丙烯酰胺凝胶电泳分析时也很明显（分子量分别为59,400、60,600、62,600和63,800）。通过等电聚焦分离为六个主要条带（等电点范围为4.40至4.82）证实了这种异质性。N端分析、用人肾素消化和去糖基化研究表明，该制剂包含几种不同糖基化程度的血管紧张素原形式。结果表明，唾液酸的存在是决定异质性的主要因素。
