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Partial purification of the phenylalanine-binding protein from Aspergillus nidulans mycelia, using Triton X-100 extraction and affinity chromatography on l-phenylalanine-CH-Sepharose, indicated that the p-fluorophenylalanine-resistant mutant, fpaD11, has a significantly reduced level of phenylalanine-binding protein compared with the wild type. This seems to be the cause of the reduced uptake of phenylalanine and consequent p-fluorophenylalanine-resistance of this mutant.
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