scholarly journals Single Turnover Kinetics of Tryptophan Hydroxylase: Evidence for a New Intermediate in the Reaction of the Aromatic Amino Acid Hydroxylases

Biochemistry ◽  
2010 ◽  
Vol 49 (35) ◽  
pp. 7563-7571 ◽  
Author(s):  
Jorge Alex Pavon ◽  
Bekir Eser ◽  
Michaela T. Huynh ◽  
Paul F. Fitzpatrick
1987 ◽  
Vol 13 (5) ◽  
pp. 575-580 ◽  
Author(s):  
Fred D. Ledley ◽  
Hernan E. Grenett ◽  
David P. Bartos ◽  
Peter Tuinen ◽  
David H. Ledbetter ◽  
...  

1988 ◽  
Vol 255 (1) ◽  
pp. 193-196 ◽  
Author(s):  
R G H Cotton ◽  
W McAdam ◽  
I Jennings ◽  
F J Morgan

PH8 monoclonal antibody has previously been shown to react with all three aromatic amino acid hydroxylases, being particularly useful for immunohistochemical staining of brain tissue [Haan, Jennings, Cuello, Nakata, Chow, Kushinsky, Brittingham & Cotton (1987) Brain Res. 426, 19-27]. Western-blot analysis of liver extracts showed that PH8 reacted with phenylalanine hydroxylase from a wide range of vertebrate species. The epitope for antibody PH8 has been localized to the human phenylalanine hydroxylase sequence between amino acid residues 139 and 155. This highly conserved region of the aromatic amino acid hydroxylases has 11 out of 17 amino acids identical in phenylalanine hydroxylase, tyrosine hydroxylase and tryptophan hydroxylase.


2004 ◽  
Vol 47 (24) ◽  
pp. 5962-5971 ◽  
Author(s):  
Knut Teigen ◽  
Khanh K. Dao ◽  
Jeffrey A. McKinney ◽  
Antonius C. F. Gorren ◽  
Bernd Mayer ◽  
...  

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