scholarly journals Determination of tryptophan oxygenase activity in rat liver homogenates

1984 ◽  
Vol 221 (2) ◽  
pp. 557-558 ◽  
Author(s):  
L Stowell ◽  
J Mørland
1983 ◽  
Vol 209 (3) ◽  
pp. 831-836 ◽  
Author(s):  
L Stowell ◽  
J Mørland

1. With two different methods for assaying the tryptophan oxygenase activity in rat liver homogenates, the effects of some methodological factors on the activity of the enzyme were studied. 2. In fed, but not in starved, rats a compound(s) absorbing at 365 nm, interfering with the reading of kynurenine absorbance, disappeared gradually during incubation. 3. A correction for this tryptophan-independent reaction was necessary in order to determine correct tryptophan oxygenase activity. 4. Blood remaining in liver tissue post mortem can serve as a source of cofactor haem for tryptophan oxygenase, causing spuriously high values for the activity of the holoenzyme form of tryptophan oxygenase. 5. A rapid and progressive activation of tryptophan oxygenase post mortem occurs in undisrupted liver tissue, and this activation is temperature-dependent.


1983 ◽  
Vol 215 (3) ◽  
pp. 709-710 ◽  
Author(s):  
A A B Badawy ◽  
C J Morgan ◽  
N R Davis

1968 ◽  
Vol 107 (4) ◽  
pp. 507-518 ◽  
Author(s):  
F. P. Van Roy ◽  
K. P. M. Heirwegh

1. Conjugated bilirubin is conveniently determined by coupling with the diazonium salt of ethyl anthranilate. 2. This method has been used in the development of assays for UDP-glucuronyltransferase (EC 2.4.1.17), with bilirubin as substrate, in rat liver homogenates, microsomal preparations and partly purified fractions. 3. Chromatographic analysis suggests that bilirubin monoglucuronide is the product of the enzyme systems studied.


1972 ◽  
Vol 46 (1) ◽  
pp. 352-355 ◽  
Author(s):  
D.J. Walton ◽  
Lauralyn M. Gauchie
Keyword(s):  

1949 ◽  
Vol 181 (1) ◽  
pp. 255-271 ◽  
Author(s):  
Dan A. Richert ◽  
Sally. Edwards ◽  
W.W. Westerfeld

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