Separation of human renin substrate from renin and a major contaminating albumin using a concanavalin A-sepharose column.

Abstract

Human plasma renin substrate was purified and separated from renin by a concanavalin A-Sepharose affinity column. Human renin substrate as well as renin were bound to concanavalin A. Renin substrate was eluted with 0.1 M D-glucose in 20 mM Tris/HCl buffer, pH 8.0. The specific activity increased from 38.5 to 653 ng of angiotensin-I equivalents per mg of protein (17-fold) and the recovery was 85%. Renin was eluted completely with 0.2 M alpha-D-methylglucoside and 0.2 M alpha-D-methylmannoside.

Cite this paper

@article{Hiwada1977SeparationOH, title={Separation of human renin substrate from renin and a major contaminating albumin using a concanavalin A-sepharose column.}, author={K. Hiwada and Hirokazu Tanaka and Kazuo Nishimura and Takako Kokubu}, journal={Clinica chimica acta; international journal of clinical chemistry}, year={1977}, volume={74 3}, pages={203-6} }