scholarly journals Chemical modification of the human ether-a-go-go-related gene (HERG) K+ current by the amino-group reagent trinitrobenzene sulfonic acid

2006 ◽  
Vol 29 (4) ◽  
pp. 310-317 ◽  
Author(s):  
Su-Hyun Jo ◽  
Se-Young Choi ◽  
Ji-Hyun Yun ◽  
Young-Sang Koh ◽  
Won-Kyung Ho ◽  
...  
Keyword(s):  
Chemical Modification ◽  
Sulfonic Acid ◽  
Trinitrobenzene Sulfonic Acid ◽  
Amino Group ◽  
Related Gene ◽  
K Current

The reaction of 2,4,6-trinitrobenzene sulfonic acid with pancreatic elastase

1970 ◽  
Vol 48 (11) ◽  
pp. 1249-1259 ◽  
Author(s):  
Leticia Rao ◽  
T. Hofmann
Keyword(s):  
Rate Constant ◽  
Sulfonic Acid ◽  
Ph Dependence ◽  
Order Rate Constant ◽  
Trinitrobenzene Sulfonic Acid ◽  
Amino Group ◽  
Tyrosine Residues ◽  
Inactivation Rate Constant ◽  
Lysine Residues ◽  
Ph Range

The reaction of elastase with trinitrobenzene sulfonic acid was investigated in the pH range 9–12. Elastase was found to be inactivated by 2,4,6-trinitrobenzene sulfonic acid. The pH dependence of the pseudo first-order inactivation rate constant showed a pK of 10.3 and gave a Hill plot coefficient of 1.15. Trinitrophenol did not inactivate the enzyme. These results indicate that the inactivation is due to the covalent reaction of trinitrobenzene sulfonic acid with a single group in the enzyme. This group is not the N-terminal since the loss of N-terminal valine was considerably slower than the loss of activity at pH 10.5. The inactivation of elastase with 2,4-dinitrofluorobenzene also showed no correlation with the loss of the N-terminal. When the enzyme was exhaustively treated and fully inactivated with trinitrobenzene sulfonic acid at pH 10.5, the N-terminal valine and two out of three lysine residues were trinitrophenylated. No evidence for the loss of histidine was found. One of the tyrosine residues may be trinitrophenylated as judged from the molar extinction of the trinitrophenylated protein, but it has not been possible to isolate a trinitrophenylated tyrosine-containing peptide. The results can be interpreted in one of two ways: (a) trinitrophenylation of a group with a pK of 10.3, not involved in the activity, inactivates because the introduction of the trinitrophenyl residue causes a denaturation of the enzyme; or (b) a group with a pK of 10.3 controls the active conformation of the enzyme. The results do not exclude the possibility that the N-terminal plays an important role in the activity of the enzyme. Below pH 10.5 the reactivity of the N-terminal is low, indicating that it is buried.At pH 9.0 only the ε-amino group of lysine in position 224 reacted with trinitrobenzene sulfonic acid and full activity was retained. The second-order rate constant for the trinitrophenylation of this group was 25 times higher than that of the ε-amino group of the α-N-benzoyllysine.

Inhibition of indoleamine 2,3-dioxygenase augments inflammation in the trinitrobenzene sulfonic acid (TNBS) colitis model in mice

2003 ◽  
Vol 124 (4) ◽  
pp. A486
Author(s):  
Gregory J. Gurtner ◽  
Rodney Newberry ◽  
Suzanne Shloemann ◽  
Keely McDonald ◽  
William F. Stenson
Keyword(s):  
Sulfonic Acid ◽  
Trinitrobenzene Sulfonic Acid ◽  
Indoleamine 2,3 Dioxygenase ◽  
Tnbs Colitis ◽  
Colitis Model

Inhibition of indoleamine 2,3-dioxygenase augments trinitrobenzene sulfonic acid colitis in mice

2003 ◽  
Vol 125 (6) ◽  
pp. 1762-1773 ◽  
Author(s):  
Gregory J Gurtner ◽  
Rodney D Newberry ◽  
Suzanne R Schloemann ◽  
Keely G McDonald ◽  
William F Stenson
Keyword(s):  
Sulfonic Acid ◽  
Trinitrobenzene Sulfonic Acid ◽  
Indoleamine 2,3 Dioxygenase

The Role of the Tumor Necrosis Factor Receptor in 2,4,6-Trinitrobenzene Sulfonic Acid (TNBS)-Induced Colitis in Mice

2005 ◽  
Vol 50 (9) ◽  
pp. 1669-1676 ◽  
Author(s):  
Minoru Nakai ◽  
Kaori Sudo ◽  
Yasuhiro Yamada ◽  
Yasushi Kojima ◽  
Tomohiro Kato ◽  
...  
Keyword(s):  
Tumor Necrosis Factor ◽  
Sulfonic Acid ◽  
Tumor Necrosis ◽  
Tumor Necrosis Factor Receptor ◽  
Trinitrobenzene Sulfonic Acid ◽  
Necrosis Factor
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