Key result
Separation of rat brain extracts on hemoglobin agarose resin yielded a >10-fold increase in renin-like specific activity and a 50% decrease in cathepsin specific activity compared to CM-cellulose.
A renin-like enzyme was successfully separated from acid protease in rat brains using hemoglobin agarose resin, with the frontal cortex showing the highest renin activity.
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Feasibility of renin-like enzyme separation shown in rat brain; leaves open translation to human cardiovascular renin research.
A renin-like enzyme was separated from acid protease (cathepsin) from whole and different parts of rat brains on hemoglobin agarose resin. During the separation steps the specific activity of the brain renin-like enzyme was increased, while the specific activity of the brain cathepsin was decreased. More than 10-folds increase in the brain renin-like specific activity, and a 50% decrease in the brain cathepsin specific activity were obtained when compared to their activities obtained when separation on CM-cellulose column occurred. The brain renin-like enzyme showed optimal activity in the range of pH 6-7. The frontal cortex showed the highest renin activity, (5.4ng Angiotensin I/g tissue/hr).
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Hassan Osman (2009) studied this question. Separation on hemoglobin agarose resin vs. Separation on CM-cellulose column was evaluated on Specific activity of brain renin-like enzyme and cathepsin. Separation of rat brain extracts on hemoglobin agarose resin yielded a >10-fold increase in renin-like specific activity and a 50% decrease in cathepsin specific activity compared to CM-cellulose.
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