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The Preparation of Crystalline Rennin^*

The Carnation Company Research Laboratories, Milwaukee, Wisconsin

ABSTRACT

Rennin has been the subject of many papers, but the evidence characterizing the chemical and physical properties of the enzyme has been highly contradictory. Conflicting views have arisen with regard to the mode of action of rennin possibly because various crude preparations as well as so-called "pure" preparations have been used. It is obviously of essential importance to obtain rennin in its highest state of purity for investigational work involving studies of the enzyme itself, its action, or the resulting product of the enzyme action

A method for the purification of rennin from commercial extract and some of the properties of the purified product were described in a recent paper by Hankinson and Palmer (2). Attempts to crystallize the highly purified protein were unsuccessful.

The crystallization of rennin was recently accomplished, however, in the course of experimentation with procedures to give a further purification with decreased losses of active material. A report of these experiments, including the relation of several recognized variables and some of the properties of crystalline rennin, is the purpose of this paper.

^* Presented at the 37th Annual Meeting, American Dairy Science Association, Michigan State College, June 25, 1942.