Abstract
THE limited digestion of ovine pituitary lactogenic hormone by chymotrypsin has recently been investigated in this laboratory1,2. It was found that preparations of prolactin showed lactogenic activity even after 50 per cent digestion with the enzyme. Ultracentrifugation investigations revealed that the prolactin core contained a component3 which had a sedimentation coefficient close to that of the non-treated hormone. The digest also contained another protein fraction which sedim nted more slowly than the bulk of the material3. This communication is concerned with the purification and properties of this latter low-molecular-weight component.
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References
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SLUYSER, M., LI, C. Preparation of a Low Molecular Weight Component with Lactogenic Activity from a Limited Chymotryptic Digest of Ovine Prolactin. Nature 200, 1007–1008 (1963). https://doi.org/10.1038/2001007a0
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DOI: https://doi.org/10.1038/2001007a0
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