1. The low-molecular-weight (40 000) form of renin was converted into the high-molecular-weight (60 000) form of renin with sulphydryl oxidation, and the high-molecular-weight form of renin was re-converted into the low-molecular-weight form with a reduction of disulphide bonds in the renal cortical homogenate of the dog. Therefore, the low- and high-molecular-weight forms of renin were interconvertible.

2. The formation of high-molecular-weight form of renin required a renin binding substance which was found to be included in the cytosol fraction of kidney cortex of the dog.

3. The renin binding substance of the dog was unstable to heat and low pH, but vitally resistant to Triton X-100 and chloroform. It did not bind to concanavalin A Sepharose 4B.

4. The renin binding substance was eluted in the molecular-weight region between 156 000 and 60 000 on Sephadex G-200, and such apparent molecular weight was not altered by urea at 4 mol/l; thus molecular weight greater than the theoretically expected value of 20 000 was indicated.

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