Incomplete process of recombinant human platelet-derived growth factor produced in yeast and its effect on the biological activity. |
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Authors: | M Calderón-Cacia P Tekamp-Olson J Allen C George-Nascimento |
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Institution: | Chiron Research Laboratories, Chiron Corporation, Emeryville, California 94608. |
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Abstract: | Partially purified recombinant human Platelet-derived Growth Factor BB homodimer isolated from yeast culture media contains variable amounts of unprocessed PDGF-BB. This unprocessed PDGF-BB is found as a result of incomplete cleavage of the precursor to form the mature protein. Although the signal peptide is efficiently removed, a fraction of the PDGF secreted has an extended sequence corresponding to the truncated yeast alpha-factor leader. The data suggest that it is the amino acid chain from the truncated a-factor leader and not the sugar moiety attached to it that is responsible for the higher mitogenic activity found in this unprocessed molecule compared to highly purified PDGF-BB. |
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