Purification, characterization and induction of L-phenylalanine ammonia-lyase in Phaseolus vulgaris
نویسندگان
چکیده
منابع مشابه
l-Phenylalanine Ammonia-Lyase Activity During Germination of Phaseolus vulgaris.
l-Phenylalanine ammonia-lyase (PAL) activity develops in excised bean axes after approximately 5 hours of incubation and reaches a maximum level after 14 hours of incubation. Light does not affect the development of activity, but puromycin, cycloheximide, actinomycin D, and 5-fluorouracil inhibit.During this period of incubation both d- and l-p-fluorophenylalanine stimulate fresh weight increas...
متن کاملPurification and Characterization of Phenylalanine Ammonia Lyase from Trichosporon cutaneum
Trichosporon cutaneum phenylalanine ammonia lyase was selected as a model to investigate the dual substrate activity of this family of enzymes. Sequencing of the PAL gene identified an extensive intron region at the N-terminus. Five amino acid residues differing from a prior report were identified. Highest Phe : Tyr activities (1.6 ± 0.3 : 0.4 ± 0.1 μ mol/h g wet weight) were induced by Tyr. ...
متن کاملThe loss of morphogenetic potential and induction of phenylalanine ammonia-lyase in suspension cultures of Phaseolus vulgaris.
The loss of morphogenetic potential in bean suspension cultures has been investigated by measuring the amounts of phenylalanine ammonia-lyase activity induced in the cells when they are transferred from a medium in which they are grown and maintained to an induction medium. The tissue has been grown in 2 types of medium: (1) supplemented with 2,4-dichlorophenoxyacetic acid as the only growth ho...
متن کاملl-Phenylalanine Ammonia-lyase (Maize): Partial Purification and Response to Gibberellic Acid and Cycloheximide of l-Phenylalanine and l-Tyrosine Ammonia-lyase Activities.
Extracts of maize leaf sheath tissue deaminate both l-phenylalanine and l-tyrosine. The activities with both substrates are enhanced by treating the plant with gibberellic acid. Both activities decrease rapidly at the same rate when tissue is incubated in a moist atmosphere, and this decrease can be slowed by treatment with cycloheximide. The ratio of the activities was constant throughout a se...
متن کاملPhenylalanine ammonia-lyase. Induction and purification from yeast and clearance in mammals.
Yeast phenylalanine ammonia-lyase (EC 4.3.1.5) catalyzes the deamination of L-phenylalanine to form trans-cinnamic acid and tyrosine to trans-coumaric acid. Maximal enzyme activity in Rhodotorula glutinis (2 units/g, wet weight, of yeast) was induced in late-log phase (12 to 14 hours) of growth in a culture medium containing 1.0% malt extract, 0.1% yeast extract, and 0.1% L-phenylalanine. A hig...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1988
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1988.tb14449.x