Covalent Binding of Catechol Estrogens to Glutathione Catalyzed by Horseradish Peroxidase, Lactoperoxidase, or Rat Liver Microsomes

1998 ◽  
Vol 11 (8) ◽  
pp. 917-924 ◽  
Author(s):  
Kai Cao ◽  
Prabu D. Devanesan ◽  
Ragulan Ramanathan ◽  
Michael L. Gross ◽  
Eleanor G. Rogan ◽  
...  
Keyword(s):  
Horseradish Peroxidase ◽  
Rat Liver ◽  
Covalent Binding ◽  
Liver Microsomes ◽  
Rat Liver Microsomes ◽  
Catechol Estrogens

Covalent binding of carbaryl (1-naphthyl-N-ethylcarbamate) to rat liver microsomes in vitro

1979 ◽  
Vol 24 (1) ◽  
pp. 1-17 ◽  
Author(s):  
Alexander Miller ◽  
Marilyn C. Henderson ◽  
Donald R. Buhler
Keyword(s):  
Rat Liver ◽  
Covalent Binding ◽  
Liver Microsomes ◽  
Rat Liver Microsomes

Characterization of covalent binding of N'-nitrosonornicotine in rat liver microsomes

1986 ◽  
Vol 7 (1) ◽  
pp. 3-8 ◽  
Author(s):  
Michael F. Hughes ◽  
William J. Brock ◽  
Lisa J. Marion ◽  
Mary Vore
Keyword(s):  
Rat Liver ◽  
Covalent Binding ◽  
Liver Microsomes ◽  
Rat Liver Microsomes

Rat liver microsomes catalyse covalent binding of 14C-vinyl chloride to macromolecules

Nature ◽  
1975 ◽  
Vol 257 (5522) ◽  
pp. 134-135 ◽  
Author(s):  
H. KAPPUS ◽  
H. M. BOLT ◽  
A. BUCHTER ◽  
W. BOLT
Keyword(s):  
Vinyl Chloride ◽  
Rat Liver ◽  
Covalent Binding ◽  
Liver Microsomes ◽  
Rat Liver Microsomes

Peroxidase-catalyzed conjugation of [4-14C] estradiol with albumin and thiols

1970 ◽  
Vol 48 (11) ◽  
pp. 1192-1198 ◽  
Author(s):  
P. H. Jellinck ◽  
Rosemarie Fletcher
Keyword(s):  
Horseradish Peroxidase ◽  
Rat Liver ◽  
Liver Microsomes ◽  
Model System ◽  
Water Soluble ◽  
Rat Liver Microsomes ◽  
Two Systems

The mechanism of conjugation of estradiol with either albumin or various thiols in the presence of horseradish peroxidase was studied and these two systems were shown to differ in a number of ways. With albumin, the reaction was slow, required Mn2+, and was inhibited by catalase but not iodoacetamide. In contrast, the reaction with thiols was rapid, did not require Mn2+, and was relatively insensitive to catalase. The yield of conjugates with different thiols and the effect of various inhibitors were also determined. The nature of the water-soluble steroid conjugate was investigated and the product obtained with glutathione shown to differ from that formed by rat liver microsomes. The possible extension of this model system to the situation existing in estrogen-stimulated uteri is discussed.

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