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.

scholarly journals Purification and immunochemical characterization of monoamine oxidase from rat and human liver

1977 ◽  
Vol 161 (1) ◽  
pp. 167-174 ◽  
Author(s):  
R G Dennick ◽  
R J Mayer
Keyword(s):  
Enzyme Activity ◽  
Monoamine Oxidase ◽  
Enzyme Activities ◽  
Gel Electrophoresis ◽  
Human Liver ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Deae Cellulose ◽  
Triton X

1. Monoamine oxidase from rat and human liver was purified to homogeneity by the criterion of polyacrylamide-gel electrophoresis in the presence of sodium dodecyl sulphate. 2. The enzyme activity was extracted from mitochondrial preparations by Triton X-100. The enzyme was purified by (NH4)2SO4 fractionation followed by chromatography on DEAE-cellulose, Sepharose 6B, spheroidal hydroxyapatite, and finally chromatography on diazo-coupled tyramine-Sepharose. 3. Distinct differences occur in the chromatographic behaviour of the two enzymes on both DEAE-cellulose and spheroidal hydroxyapatite. 4. It is unlikely that the purification of the enzymes on tyramine-Sepharose is due to affinity chromatography and reasons for this are discussed. 5. The purified enzymes did not oxidize-5-hydroxytryptamine and the relative activities of the enzymes with benzylamine were increased approx. 1.25-fold compared with the enzyme activities of mitochondrial preparations. 6. Immunotitration of enzyme activity in extracts of mitochondrial preparations from rat liver was carried out with 5-hydroxytryptamine, tyramine and benzylamine. The enzyme activities were completely immunoprecipitated by the same volume of antiserum. Similar results were obtained with the antiserum to the enzyme from human liver.

scholarly journals Characterization of antibody against human liver guanase by immunoblotting and immunohistochemical staining of human liver guanase by a direct labeling antibody-enzyme method.

1989 ◽  
Vol 37 (5) ◽  
pp. 611-615 ◽  
Author(s):  
S Ito ◽  
A Iwasaki ◽  
J Syundo ◽  
Y Tamura ◽  
S Kishi ◽  
...  
Keyword(s):  
Liver Enzyme ◽  
Specific Antibody ◽  
Immunohistochemical Staining ◽  
Human Liver ◽  
Liver Extract ◽  
Precipitin Line ◽  
Tissue Sections ◽  
Immunohistochemical Reaction ◽  
Enzyme Method

Human liver guanase was purified and a specific antibody against it was raised in rabbits. The antiserum formed a single precipitin line with human liver extract, and also completely inhibited the activity of the liver enzyme. An immunoblotting study showed that the antibody bound specifically to one band of protein with guanase activity and not to other proteins. Therefore, we concluded that this antiserum against the liver enzyme was suitable for use in immunohistochemical demonstration of guanase. In tissue sections, the immunohistochemical reaction with this antibody was positive in the same locations as the histochemical guanase reaction with DAB (3,3'-diaminobenzidine tetrahydrochloride).

scholarly journals The vectorial orientation of human monoamine oxidase in the mitochondrial outer membrane

1979 ◽  
Vol 181 (1) ◽  
pp. 7-14 ◽  
Author(s):  
S M Russell ◽  
J Davey ◽  
R J Mayer
Keyword(s):  
Monoamine Oxidase ◽  
Outer Membrane ◽  
Outer Surface ◽  
Human Liver ◽  
Brain Cortex ◽  
Mitochondrial Outer Membrane ◽  
Inner Surface

1. The localization of monoamine oxidase in the mitochondrial outer membrane was studied in preparations of human liver mitochondrial and brain-cortex non-synaptosomal and synaptosomal mitochondria. 2. Immunochemical accessibility in iso-osmotic and hypo-osmotic mitochondrial preparations was used to localize the enzyme. 3. It was shown that the immunochemically accessible tyramine-oxidizing activity was distributed approximately equally on both surfaces of the membrane in human liver and brain-cortex non-synaptosomal mitochondria. However, the immunochemically accessible beta-phenethylamine-oxidizing activity was situated predominantly on the outer surface, and the immunochemically accessible 5-hydroxytryptamine-oxidizing activity was situated predominantly on the inner surface of the mitochondrial outer membrane in liver and brain-cortex non-synaptosomal mitochondrial preparations. 4. Considerable variation in the distribution of the enzyme in preparations of synaptosomal mitochondria was seen. 5. The simplest model consistent with our observations is that, in liver and brain-cortex non-synaptosomal mitochondria, the tyramine-oxidizing activity is distributed on both sides of the mitochondrial outer membrane, the beta-phenethylamine-oxidizing activity is located on the outer surface of the outer membrane and the 5-hydroxytryptamine-oxidizing activity is located on the inner surface of the mitochondria outer membrane

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 human liver and heart ferritins with monoclonal antibodies

1986 ◽  
Vol 872 (1-2) ◽  
pp. 61-71 ◽  
Author(s):  
Alessandra Luzzago ◽  
Paolo Arosio ◽  
Carmelo Iacobello ◽  
Giuseppina Ruggeri ◽  
Lorenzo Capucci ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Human Liver ◽  
Immunochemical Characterization
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