Abstract
AbstractIt was shown that a specimen of crystallized rennin was inhomogeneous, and that a homogeneous rennin could be separated by means of the diethylaminoethyl cellulose ion exchange chromatography. The pure enzyme was characterized by determining its terminal amino acids, and by spectropolarimetry. Rennin behaved abnormally with respect to optical rotatory dispersion, an indication of peculiar structure and configuration of this protein.
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