Identification of tyrosine hydroxylase as a physiological substrate for Cdk5
โ Scribed by Janice W. Kansy; S. Colette Daubner; Akinori Nishi; Naoki Sotogaku; Michael D. Lloyd; Chan Nguyen; Lin Lu; John W. Haycock; Bruce T. Hope; Paul F. Fitzpatrick; James A. Bibb
- Book ID
- 111178499
- Publisher
- John Wiley and Sons
- Year
- 2004
- Tongue
- English
- Weight
- 309 KB
- Volume
- 91
- Category
- Article
- ISSN
- 0022-3042
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We have recently determined that -Ile-Tyr- were the two critical residues as a peptide substrate for p60c-src protein tyrosine kinase (Lou, Q. et al., Lett. Peptide Sci., 1995, 2, 289). Here, we report on the design and synthesis of a secondary 'one-bead, one-compound' combinatorial peptide library
Tyrosine hydroxylase (TH) activity can be modified by changes in the specific activity of the enzyme (SA TH ) or in the levels of active enzyme. We developed a methodology making it possible to measure with excellent anatomical resolution TH enzymatic activity and TH protein quantity by quantitative