scholarly journals Purification and immunochemical characterization of a male-specific rat liver oestrogen sulphotransferase

1993 ◽  
Vol 289 (3) ◽  
pp. 719-725 ◽  
Author(s):  
E B Borthwick ◽  
A Burchell ◽  
M W Coughtrie
Keyword(s):  
Rat Liver ◽  
Human Liver ◽  
Regulatory Mechanism ◽  
Biologically Active ◽  
Male Rats ◽  
Immunochemical Characterization ◽  
Male Specific ◽  
The Brain ◽  
Brain Examination

Sulphation of oestrogens represents an important regulatory mechanism for these biologically active compounds. We have characterized and purified a form of rat liver sulphotransferase (ST), existing as a 32,500 Da monomer, which sulphates oestrogens, and have used this preparation to produce antibodies against oestrogen ST. The enzyme was active against oestrone, oestriol and beta-oestradiol, but not towards androgens. Using the antibody as a probe for immunoblotting, it was determined that the enzyme is expressed solely in male rats, and predominantly in the liver. Of the tissues examined, the only major extrahepatic tissue found to have any oestrogen ST was the brain (although the levels were very low), indicating that there might be a role for the sulphation of oestrogens in the brain. Examination of human liver and platelet cytosols by immunoblotting showed that the antibody recognized two major proteins of 32 and 34 kDa, which were presumed to correspond to the two principal phenol ST isoenzymes present in man.

Immunochemical characterization of protein kinase C in rat liver nuclei and subnuclear fractions

1987 ◽  
Vol 142 (2) ◽  
pp. 367-375 ◽  
Author(s):  
Silvano Capitani ◽  
Peggy R. Girard ◽  
Gonzalo J. Mazzei ◽  
J.F. Kuo ◽  
Ronald Berezney ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Rat Liver ◽  
Immunochemical Characterization ◽  
Rat Liver Nuclei ◽  
Kinase C ◽  
Liver Nuclei

Immunochemical characterization of cytochrome P-450 isozymes responsible for benzene oxidation in the rat liver

1989 ◽  
Vol 10 (9) ◽  
pp. 1713-1717 ◽  
Author(s):  
Tamie Nakajima ◽  
Eivor Elovaara ◽  
Sang S. Park ◽  
Harry V. Gelboin ◽  
Eino Hietanen ◽  
...  
Keyword(s):  
Rat Liver ◽  
Benzene Oxidation ◽  
Immunochemical Characterization ◽  
Cytochrome P 450

GESCHLECHTSSPEZIFIKA DER BIOSYNTHESE VON STEROIDGLUCURONIDEN IN DER MIT TESTOSTERON PERFUNDIERTEN RATTENLEBER

1970 ◽  
Vol 63 (1) ◽  
pp. 59-68 ◽  
Author(s):  
Herbert Schriefers ◽  
Rüdiger Ghraf ◽  
Mathilde Brodesser
Keyword(s):  
Rat Liver ◽  
Glucuronic Acid ◽  
Biologically Active ◽  
Female Rats ◽  
Male Rats ◽  
Glucuronyl Transferase ◽  
Minor Part ◽  
Type C ◽  
Male Sex ◽  
Free Steroid

ABSTRACT In order to reveal contingent sex specificities regarding the biosynthesis of steroid glucuronides perfusion experiments with rat liver and [4-14C] testosterone** as substrate were carried out. 75% (male rats) respectively 89% (female rats) of the chromatographically isolated aglucones could be identified. In the course of one single passage of the substrate the female liver retains significantly more (factor 1.4) 14C-activity than the male. Since this phenomenon is not due to a sex different capacity of the liver for the synthesis of steroid glucuronides, it must be regarded as a sex characteristic sui generis. The aglucone pattern exhibits the following sex differences: The quantitatively predominant aglucones are testosterone (47%) and hydroxylated Δ4-3-ketosteroids in male rats and ring A hydrogenated products of the type C19O2 (80.7%) in females. Within the group of ring A hydrogenated C19O2-aglucones the biologically inactive 5β-compounds (5β-androsterone, 17β-hydroxy-5β-androstan-3-one, 5β-androstane-3α, 17β-diol) prevail in the male sex, and the biologically active 5α-compounds (5α-androsterone, 17β-hydroxy-5α-androstan-3-one, 5α-androstane-3α, 17β-diol) in the female sex. With either sex the percentage share of 5α- and 5β-androsterone and 5α- and 5β-androstane-3α,17β-diol in the glucuronide fraction is extremely higher than in the fraction of free steroids though the affinity of the UDP-glucuronyl transferase of the rat liver is considerably lower for these four metabolites than for the 4,5-dihydro-testosterone derivatives which, however, for their part are nearly equally distributed between the glucuronide and the free steroid fraction. Therefore, it can be postulated that the glucuronides of the above mentioned androsterones and androstanediols derive mainly from the hydrogenation of testosterone glucuronide and only for the minor part from direct conjugation of the hydrogenation products with glucuronic acid.

scholarly journals Immunochemical characterization of monoamine oxidase from human liver, placenta, platelets and brain cortex

1979 ◽  
Vol 181 (1) ◽  
pp. 15-20 ◽  
Author(s):  
S M Russell ◽  
J Davey ◽  
R J Mayer
Keyword(s):  
Enzyme Activity ◽  
Monoamine Oxidase ◽  
Liver Enzyme ◽  
Human Liver ◽  
Brain Cortex ◽  
Lipid Binding ◽  
Mitochondrial Preparation ◽  
Immunochemical Characterization ◽  
Immunodiffusion Analysis

1. Antiserum raised to purified human liver monoamine oxidase was used to characterize the monoamine oxidase from human liver, brain cortex, placenta and platelets. 2. Antibodies to monoamine oxidase were purified by adsorption with a mitochondrial preparation. 3. Monoamine oxidase was present in liver particle-free supernatant as measured by enzyme activity and immunodiffusion. 4. Multiple precipitin lines were obtained on immunodiffusion analysis against the purified liver enzyme. It is proposed that this is due to either aggregation or to differential lipid binding. 5. The results suggest that the functionally different enzymes found in liver, brain cortex, platelets and placenta are immunochemically related and may be identical.

Purification and immunochemical characterization of the cytoplasmic androgen-binding protein of rat liver

Biochemistry ◽  
1989 ◽  
Vol 28 (4) ◽  
pp. 1732-1736 ◽  
Author(s):  
William F. Demyan ◽  
Fazlul H. Sarkar ◽  
C. V. Ramana Murty ◽  
Arun K. Roy
Keyword(s):  
Rat Liver ◽  
Binding Protein ◽  
Immunochemical Characterization ◽  
Androgen Binding Protein ◽  
Androgen Binding
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