摘要: Summary Block-shaped crystals were prepared from a concentrated solution of purified rennin by dialyzing it against Berridge's salting-in buffer. The purification procedure was relatively simple, and proved successful in each several attempts to obtain pure enough crystallize. A single boundary electrophoresis represented over 96% the protein when dissolved run at pH 6.8 sodium phosphate buffer an ionic strength 0.2. However, least four components evident same 0.033 strength. These results show that preparations can not be considered homogeneous on basis their crystalline form or electrophoretic behavior buffers high
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