scholarly journals Determination of tryptophan pyrrolase activity in rat liver homogenates

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

scholarly journals Tryptophan pyrrolase in haem regulation. Experiments with administered haematin and the relationship between the haem saturation of tryptophan pyrrolase and the activity of 5-aminolaevulinate synthase in rat liver

1980 ◽  
Vol 192 (2) ◽  
pp. 403-410 ◽  
Author(s):  
A N Welch ◽  
A A B Badawy
Keyword(s):  
Rat Liver ◽  
Initial Phase ◽  
Inverse Relationship ◽  
Tryptophan Pyrrolase ◽  
Liver Homogenates ◽  
The Relationship

1. Administration of haematin to rats decreases 5-aminolaevulinate synthase activity in whole liver homogenates. 2. An inverse relationship between this decrease and the increase in saturation of apo-(tryptophan pyrrolase) with haem is observed during the initial phase of treatment with haematin. 3. Significant changes in both functions are caused by a 1 mg/kg dose of haematin, whereas the maximum effects are achieved by the 5 mg/kg dose. 4. Prevention by allopurinol of the conjugation of exogenously administered haematin with apo-(tryptophan pyrrolase) renders this haem available for further repression of 5 aminolaevulinate synthase. 5. The various aspects of the relationship between synthase activity and the haem saturation of tryptophan pyrrolase are discussed.

scholarly journals Tryptophan pyrrolase in haem regulation. The relationship between the depletion of rat liver tryptophan pyrrolase haem and the enhancement of 5-aminolaevulinate synthase activity by 2-allyl-2-isopropylacetamide

1980 ◽  
Vol 186 (3) ◽  
pp. 763-772 ◽  
Author(s):  
A A B Badawy ◽  
C J Morgan
Keyword(s):  
Rat Liver ◽  
Activity Maximum ◽  
Haem Biosynthesis ◽  
Hexobarbital Sleeping Time ◽  
Tryptophan Pyrrolase ◽  
Liver Homogenates ◽  
The Relationship ◽  
Cytochrome P 450 ◽  
Phenazine Methosulphate

Rat liver tryptophan pyrrolase haem is maximally depleted at 30 min after administration of a 400 mg/kg dose of 2-allyl-2-isopropylacetamide. This depletion lasts for 24 h, by which time 5-aminoleevulinate synthase activity becomes maximally enhanced. 2. though the above maximum depletion of pyrrolase haem (at 0.5h) is also produced by a 100 mg/kg dose of the porphyrogen, this does not enhance synthase activity at 24 h. It and smaller doses, however, cause a smaller but earlier enhancement of synthase activity (maximum at 2 h) and produce a similarly short-lived deplation of pyrrolase haem. 3. The depletion of pyrrolase haem and the enhancement of synthase activity by the porphyrogen are inhibited by compound SKF 525-A and phenazine methosulphate, and are potentiated by nicotinamide but not by phenobarbitone. Phenazine methosulphate and nicotinamide also exert opposite effects on hexobarbital sleeping-time. 4. 2-Allyl-2-isopropylacetamde also the depletes pyrrolase haem in vitro. It does so in liver homogenates of control rats in the presence, and in those of phenobarbitone-treated rats in the absence of added NADPH. 5. A discussion of the present results in relation to previous work with other haemoproteins suggests that, whereas cytochrome P-450 (haem) is primarily involved in the production of the active (porphyrogenic) metabolite(s) of 2-allyl-2-isopropylacetamide, the haem pool used by tryptophan pyrrolase may play an important role in the effects of this compound on haem biosynthesis.

scholarly journals Determination of bilirubin glucuronide and assay of glucuronyltransferase with bilirubin as acceptor

1968 ◽  
Vol 107 (4) ◽  
pp. 507-518 ◽  
Author(s):  
F. P. Van Roy ◽  
K. P. M. Heirwegh
Keyword(s):  
Rat Liver ◽  
Chromatographic Analysis ◽  
Diazonium Salt ◽  
Enzyme Systems ◽  
Liver Homogenates ◽  
Conjugated Bilirubin

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.

Determination of trioses in tungstate supernatants of rat liver homogenates

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

scholarly journals ON THE DETERMINATION OF LIVER XANTHINE OXIDASE AND THE RESPIRATION OF RAT LIVER HOMOGENATES

1949 ◽  
Vol 181 (1) ◽  
pp. 255-271 ◽  
Author(s):  
Dan A. Richert ◽  
Sally. Edwards ◽  
W.W. Westerfeld
Keyword(s):  
Xanthine Oxidase ◽  
Rat Liver ◽  
Liver Homogenates

scholarly journals THE INCORPORATION OF THE CARBOXYL CARBON FROM ACETATE INTO CHOLESTEROL BY RAT LIVER HOMOGENATES

1954 ◽  
Vol 206 (1) ◽  
pp. 471-481 ◽  
Author(s):  
Ivan D. Frantz ◽  
Nancy L.R. Bucher ◽  
Henny S. Schneider ◽  
Naomi H. McGovern ◽  
Ruth Kingston
Keyword(s):  
Rat Liver ◽  
Liver Homogenates ◽  
Carboxyl Carbon

scholarly journals Effect of Cytoplasmic Particles on Tryptophan Pyrrolase Activity of Rat Liver

1966 ◽  
Vol 241 (2) ◽  
pp. 304-308
Author(s):  
Olga Greengard ◽  
N. Mendelsohn ◽  
G. Acs
Keyword(s):  
Rat Liver ◽  
Tryptophan Pyrrolase
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