Human plasma contains an inactive form of renin with a m.w. of 55,000, as against around 40,000 for active human renin. After acidification to pH 3.0 or incubation with trypsin, the inactive renin becomes more active and the molecular weight falls to that of active renin. In human kidney extracts, an increase in renin concentration also occurred after acidification. The inactive form of renin may be similar to that of rabbit kidneys, which contain an inactive renin that can be activated by removal of an acid-labile inhibitor. The question as to whether the inactive material is a renin proenzyme is discussed.