Inhibition of lysine utilization in bacteria by S-(beta-aminoethyl) cysteine and its reversal by lysine peptides.
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When a relaxin preparation was subjected to counter-current distribution for 355 transfers in a butanol-trichloroacetic acid system, significant biological activity was found over a band appreciably wider than was expected for a single component. By refractionation of the active band, three peptides with relaxin activity were isolated.
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