N-Acetyltransferases of Rat Liver and Blood: Substrate Specificities

Enzyme ◽  
1980 ◽  
Vol 25 (5) ◽  
pp. 309-315 ◽  
Author(s):  
R. Gollamudi ◽  
B. Muniraju ◽  
E.C. Schreiber
Keyword(s):  
Rat Liver ◽  
Substrate Specificities ◽  
Rat Liver And Blood

Substrate specificities of a bacterial sialidase and rat liver ganglioside GM3 sialyltransferase

1987 ◽  
Vol 4 (3) ◽  
pp. 291-295 ◽  
Author(s):  
D Klein ◽  
G Pohlentz ◽  
G Schwarzmann ◽  
K Sandhoff
Keyword(s):  
Rat Liver ◽  
Ganglioside Gm3 ◽  
Substrate Specificities

scholarly journals A kinetic evaluation of monoamine oxidase activity in rat liver mitochondrial outer membranes

1974 ◽  
Vol 139 (3) ◽  
pp. 645-652 ◽  
Author(s):  
Miles D. Houslay ◽  
Keith F. Tipton
Keyword(s):  
Monoamine Oxidase ◽  
Rat Liver ◽  
Oxidase Activity ◽  
Monoamine Oxidase Activity ◽  
Irreversible Inhibitor ◽  
Kinetic Evaluation ◽  
Reversible Inhibitors ◽  
Substrate Specificities ◽  
Outer Membranes ◽  
Enzyme Species

1. A preparation of mitochondrial outer membranes from rat liver can be shown to contain two kinetically distinct monoamine oxidase activities. These activities are distinguishable by their different sensitivities to the irreversible inhibitor clorgyline, and by the effect of the reversible inhibitors benzyl cyanide and 4-cyanophenol. 2. The substrate specificities of the preparation and the two enzyme species have been elucidated.

scholarly journals Isoenzymes of glutathione transferase in rat kidney cytosol

1985 ◽  
Vol 230 (3) ◽  
pp. 609-615 ◽  
Author(s):  
C Guthenberg ◽  
H Jensson ◽  
L Nyström ◽  
E Österlund ◽  
M K Tahir ◽  
...  
Keyword(s):  
Rat Liver ◽  
Liver Enzymes ◽  
Glutathione Transferase ◽  
Ethacrynic Acid ◽  
Rat Kidney ◽  
Glutathione Transferases ◽  
Substrate Specificities ◽  
Additional Peak ◽  
Rat Kidney Cytosol ◽  
Rat Liver Cytosol

Glutathione transferases from rat kidney cytosol were purified about 40-fold by chromatography on S-hexylglutathione linked to epoxy-activated Sepharose 6B. Further purification by fast protein liquid chromatography with chromatofocusing in the pH interval 10.6-7.6 resolved five major peaks of activity with 1-chloro-2,4-dinitrobenzene as the second substrate. Four of the peaks were identified with rat liver transferases 1-1, 1-2, 2-2 and 4-4 respectively. The criteria used for identification included physical properties, reactions with specific antibodies, substrate specificities and sensitivities to several inhibitors. The fourth major peak is a ‘new’ form of transferase, which has not been found in rat liver. This isoenzyme, glutathione transferase 7-7, has a lower apparent subunit Mr than any of the transferases isolated from rat liver cytosol, and does not react with antibodies raised against the liver enzymes. Glutathione transferases 3-3 and 3-4, which are abundant in liver, were only present in very small amounts. In a separate chromatofocusing separation in a lower pH interval, an additional peak was eluted at pH 6.3. This isoenzyme is characterized by its high activity with ethacrynic acid.

scholarly journals 3Rs friendly study designs facilitate rat liver and blood micronucleus assays andPig‐agene mutation assessments: Proof‐of‐concept with 13 reference chemicals

2019 ◽  
Vol 60 (8) ◽  
pp. 704-739 ◽  
Author(s):  
Stephen D. Dertinger ◽  
Svetlana L. Avlasevich ◽  
Dorothea K. Torous ◽  
Priyanka Singh ◽  
Sumee Khanal ◽  
...  
Keyword(s):  
Rat Liver ◽  
Proof Of Concept ◽  
Study Designs ◽  
Rat Liver And Blood
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