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Journal Abstract Search

264 related items for PubMed ID: 7384643

  • 1.
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  • 2. Preparation of immobilized L-phenylalanine ammonia-lyase in tubular form for depletion of L-phenylalanine.
    Pedersen H, Horvath C, Ambrus CM.
    Res Commun Chem Pathol Pharmacol; 1978 Jun; 20(3):559-69. PubMed ID: 674832
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  • 3. In vivo safety of hollow fiber enzyme-reactors with immobilized phenylalanine ammonia-lyase in a large animal model for phenylketonuria.
    Ambrus CM, Sharma SD, Horváth C, Kalghatgi K, Anthone S, Ambrus JL, Cooley C, Mirand EA.
    J Pharmacol Exp Ther; 1983 Mar; 224(3):598-602. PubMed ID: 6681841
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  • 4. Depletion of phenylalanine in the blood of phenylketonuric patients using a PAL-enzyme reactor. An in vitro study.
    Ambrus CM, Horváth C, Kalghatgi K, Clowsley M, Huzella C, Warner R, Ambrus JL, Cooley CM, Mirand EA.
    Res Commun Chem Pathol Pharmacol; 1982 Jul; 37(1):105-11. PubMed ID: 7122995
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  • 6. An extracorporeal hollow-fiber reactor for phenylketonuria using immobilized phenylalanine ammonia lyase.
    Larue C, Munnich A, Charpentier C, Saudubray JM, Frézal J, Rémy MH, Rivat C.
    Dev Pharmacol Ther; 1986 Jul; 9(2):73-81. PubMed ID: 3956347
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  • 13. Cross-linked enzyme aggregates of phenylalanine ammonia lyase: novel biocatalysts for synthesis of L-phenylalanine.
    Cui JD, Zhang S, Sun LM.
    Appl Biochem Biotechnol; 2012 Jun; 167(4):835-44. PubMed ID: 22622644
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  • 14. Phenylalanine ammonia-lyase: enzymic conversion of 3-(1,4-cyclohexadienyl)-L-alanine to trans-3-(1,4-cyclohexadienyl)acrylic acid.
    Hanson KR, Havir EA, Ressler C.
    Biochemistry; 1979 Apr 17; 18(8):1431-8. PubMed ID: 427124
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  • 15. The effect of proteinases on phenylalanine ammonia-lyase from the yeast Rhodotorula glutinis.
    Gilbert HJ, Jack GW.
    Biochem J; 1981 Dec 01; 199(3):715-23. PubMed ID: 7041889
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  • 16. [Phenylalanine ammonia-lyase of pigmented yeasts].
    Mushi NIu, Kupletskaia MB, Bab'eva IP, Egorov NS.
    Mikrobiologiia; 1980 Dec 01; 49(2):269-73. PubMed ID: 7393004
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  • 17. L-Phenylalanine ammonia-lyase (maize, potato, and Rhodotorula glutinis) Explaining the kinetic effects of substrate modification by linear free-energy relationships.
    Hanson KR, Havir EA.
    Arch Biochem Biophys; 1977 Apr 15; 180(1):102-13. PubMed ID: 558738
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  • 20. Efficient preparation of enantiopure D-phenylalanine through asymmetric resolution using immobilized phenylalanine ammonia-lyase from Rhodotorula glutinis JN-1 in a recirculating packed-bed reactor.
    Zhu L, Zhou L, Huang N, Cui W, Liu Z, Xiao K, Zhou Z.
    PLoS One; 2014 Apr 15; 9(9):e108586. PubMed ID: 25268937
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