Murakami K, Inagami T, Haas E
Circ Res. 1977 Oct;41(4 Suppl 2):4-7. doi: 10.1161/01.res.41.4.4.
An affinity gel for the purification of renin was prepared by coupling pepstatin to aminohexylagarose gel. Partially purified human renin (Haas et al., Arch. Biochem. Biophys., 110, 534-543, 1965) was purified further by affinity chromatography on the pepstatin-aminohexyl-agarose gel, gel filtration on a Sephadex G-75 column, and ion exchange chromatography on a DEAE-cellulose column. Separation from a protease permitted further purification without progressive loss of activity. Three peaks of enzymatically active renin were obtained after the DEAE-cellulose chromatography, with specific activities ranging from 206 to 166 and 85 Goldblatt units/mg protein, respectively. The specific activity of 206 GU units/mg represents a 103,000-fold purification compared to the renin present in the first crude extract.
通过将胃蛋白酶抑制剂偶联到氨基己基琼脂糖凝胶上制备了一种用于纯化肾素的亲和凝胶。部分纯化的人肾素（哈斯等人，《生物化学与生物物理学报》，110, 534 - 543, 1965）通过在胃蛋白酶抑制剂 - 氨基己基 - 琼脂糖凝胶上进行亲和层析、在葡聚糖凝胶G - 75柱上进行凝胶过滤以及在DEAE - 纤维素柱上进行离子交换层析进一步纯化。与一种蛋白酶分离后实现了进一步纯化且没有活性的逐步丧失。在DEAE - 纤维素层析后获得了三个具有酶活性的肾素峰，其比活性分别为206、166和85戈德布拉特单位/毫克蛋白质。206 GU单位/毫克的比活性相较于最初粗提物中的肾素而言代表了103,000倍的纯化。
