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.

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

scholarly journals Soluble forms of alpha-d-mannosidases from rat liver. Separation and characterization of two enzymic forms with different substrate specificities

1994 ◽  
Vol 223 (1) ◽  
pp. 99-106 ◽  
Author(s):  
Thierry GRARD ◽  
Agnes SAINT-POL ◽  
Jean-Francois HAEUW ◽  
Catherine ALONSO ◽  
Jean-Michel WIERUSZESKI ◽  
...  
Keyword(s):  
Rat Liver ◽  
Substrate Specificities

scholarly journals Substrate specificity and characterization of rat liver p-nitrophenol, 3 α-hydroxysteroid and 17 β-hydroxysteroid UDP-glucuronosyltransferases

1986 ◽  
Vol 238 (1) ◽  
pp. 65-73 ◽  
Author(s):  
C N Falany ◽  
M D Green ◽  
E Swain ◽  
T R Tephly
Keyword(s):  
Amino Acid ◽  
Rat Liver ◽  
Limited Proteolysis ◽  
Enzymic Activity ◽  
Substrate Specificities ◽  
Endogenous Substrate ◽  
Udp Glucuronosyltransferase ◽  
Endogenous Substrates ◽  
Peptide Maps

Purified preparations of rat liver 17-hydroxysteroid, 3-hydroxyandrogen and p-nitrophenol (3-methylcholanthrene-inducible) UDP-glucuronosyltransferases were further characterized as to their substrate specificities, phospholipid-dependency and physical properties. The two steroid UDP-glucuronosyltransferases were shown to exhibit strict stereospecificity with respect to the conjugation of steroids and bile acids. These enzymes have been renamed 17 beta-hydroxysteroid and 3 alpha-hydroxysteroid UDP-glucuronosyltransferase to reflect this specificity for important endogenous substrates. An endogenous substrate has not yet been identified for the p-nitrophenol (3-methylcholanthrene-inducible) UDP-glucuronosyltransferase. The steroid UDP-glucuronosyltransferase activities were dependent on phospholipid for maximal catalytic activity. Complete delipidation rendered the UDP-glucuronosyltransferases inactive, and enzymic activity was not restored when phospholipid was added to the reaction mixture. After partial delipidation, phosphatidylcholine was the most efficient phospholipid for restoration of enzymic activity. Partial delipidation also altered the kinetic parameters of the 3 alpha-hydroxysteroid UDP-glucuronosyltransferase. The three purified UDP-glucuronosyltransferases are separate and distinct proteins, with different amino acid compositions and peptide maps generated by limited proteolysis with Staphylococcus aureus V8 proteinase. Some similarity was observed between the amino acid composition and limited proteolytic maps of the steroid UDP-glucuronosyltransferases, suggesting they are more closely related to each other than to the p-nitrophenol UDP-glucuronosyltransferase.

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