Subject(s)
Angiotensin-Converting Enzyme Inhibitors/pharmacology , Blood Pressure/drug effects , Enalapril/analogs & derivatives , Peptidyl-Dipeptidase A/metabolism , Angiotensin-Converting Enzyme Inhibitors/chemical synthesis , Animals , In Vitro Techniques , Male , Medulla Oblongata/enzymology , Microsomes/enzymology , Peptidyl-Dipeptidase A/blood , Pituitary Gland/enzymology , Rats , Rats, WistarABSTRACT
Various modifications of enzyme immunoassay (EIA) for measuring kallikrein-kinin system components (bradykinin, kininogen, kallikrein) are considered. Bradykinin assays are analyzed in detail: double antibodies and competitive solid-phase EIA techniques with the use of various enzymic labels. Special attention is paid to the solid-phase variant in polymeric microplates, the simplest technique that holds good promise for clinical application. The authors have used this method for bradykinin measurements and tried to improve its sensitivity.
Subject(s)
Bradykinin/analysis , Immunoenzyme TechniquesABSTRACT
Bradykinin coupled to bovine serum albumin or to rabbits erythrocytes was used to immunize rabbits. It was shown that enzyme-linked immunosorbent assay (ELISA) has been successfully used for the investigation of the obtained immune sera.
Subject(s)
Antibody Specificity , Bradykinin/immunology , Immune Sera/isolation & purification , Animals , Antibodies/analysis , Erythrocytes/immunology , Immune Sera/analysis , Immunization , Immunoenzyme Techniques , Male , Rabbits , Serum Albumin, Bovine/immunologySubject(s)
Blood Pressure , Bradykinin/immunology , Erythrocytes/immunology , Immunization , Kallikreins/blood , Kinins/blood , Animals , Antibody Formation , Male , RabbitsSubject(s)
Blood Pressure/drug effects , Bradykinin/immunology , Immunization , Kallikreins/blood , Kinins/blood , Renin-Angiotensin System/drug effects , Animals , Antibodies/analysis , Male , Peptidyl-Dipeptidase A/blood , Prekallikrein/analysis , Rabbits , Serum Albumin, Bovine/immunology , Time FactorsABSTRACT
Aggressive behaviour (muricidal) induced in rats by local electrolyte lesions of septal brain area was accompanied by changes in angiotensin-converting enzyme (ACE) and total kinin-destroying activity (KDA) in different brain regions. In 2-month-old rats (30 days after septal operation) a decrease in ACE activity was observed in hypothalamus and striatum, while in the cerebellum the activity was increased. KDA in this group of aggressive rats was markedly increased in the pituitary body, hypothalamus and striatum. Half a year after septal lesion in spite of aggressive behaviour retention, ACE activity and KDA did not differ from their activity in nonmuricidal rats of the same age. These data show a distinct role of the peptides studied in the formation and maintenance of muricidal behaviour in rats of different age.
Subject(s)
Aggression/physiology , Aging/metabolism , Angiotensin II/metabolism , Brain/enzymology , Kinins/metabolism , Animals , Bradykinin/metabolism , Brain/surgery , Male , Mice , Peptidyl-Dipeptidase A/metabolism , Rats , Reaction Time/physiologyABSTRACT
Spontaneously muricidal rats (SMR) were selected from a group of white male rats. In the remaining animals muricide was induced by the local electrolyte damage of the brain septal area. Both muricidal models had different physiological indexes of aggressive reactions. In SMR a significant decrease in angiotensin-converting enzyme activity was detected in the midbrain and thalamus-hypothalamus areas. In the group of operated muricidal ("septal") rats alterations in angiotensin-converting enzyme activity have been revealed in none of the brain areas examined. The increase in total kinin-destroying activity in the pituitary, cerebellum, striatum and thalamus-hypothalamus areas was detected. The results indicate neurochemical specificity of brain angiotensin II and kinins in the regulation of different muricidal models.
Subject(s)
Aggression/physiology , Angiotensin II/metabolism , Bradykinin/metabolism , Brain/enzymology , Dominance, Cerebral/physiology , Limbic System/physiology , Animals , Electrolysis , Male , Mice , Peptidyl-Dipeptidase A/metabolism , RatsABSTRACT
Kinin-damaging activity (KDA) has been studied in 8 brain areas of normotensive rats and rats with spontaneous hypertension, aged 3 to 12 months. A significant depression in KDA was revealed in midbrain, striatum, thalamus, and pituitary body of normotensive rats 6 months of age, as compared to 3-month-old animals. A tendency towards KDA increase was noted in the hypothalamus. In 12-month-old normotensive rats KDA level returned to baseline (3 months of age). Comparison of KDA in rats with spontaneous hypertension aged 3 to 12 months has revealed no age-dependent differences and it is, therefore, believed that rats with spontaneous hypertension lack certain mechanisms inducing a considerable decrease of KDA in 6-month-old normotensive rats.
Subject(s)
Brain/enzymology , Hypertension/enzymology , Kinins/metabolism , Aging , Animals , Blood Pressure , Bradykinin/metabolism , Male , Rats , Rats, Inbred SHR , Rats, Inbred Strains , Tissue DistributionABSTRACT
A procedure is described for immobilization of partially purified histidase by means of covalent binding of the enzyme with amino ethyl cellulose activated by glutaraldehyde. The preparation obtained was stable within 6 months at 5 degrees and within 40 days at 39 degrees. The preparation of immobilized histidase might be used for enzymatic synthesis of urocanic acid from histidine.
Subject(s)
Ammonia-Lyases/metabolism , Histidine Ammonia-Lyase/metabolism , Histidine/metabolism , Imidazoles/biosynthesis , Liver/metabolism , Urocanic Acid/biosynthesis , Acrylic Resins , Animals , Cellulose/analogs & derivatives , Enzymes, Immobilized/metabolism , Female , Glutaral , Hydrogen-Ion Concentration , Rats , TemperatureSubject(s)
Asparaginase , Animals , Antineoplastic Agents , Asparaginase/administration & dosage , Asparaginase/therapeutic use , Asparagine , Catalysis , Chemical Phenomena , Chemistry , Drug Stability , Enzymes, Immobilized , Escherichia coli/enzymology , Hydrogen-Ion Concentration , Leukemia, Experimental/drug therapy , Leukemia, Lymphoid/drug therapy , Lymphoma, Large B-Cell, Diffuse/drug therapy , Lymphoma, Non-Hodgkin/drug therapy , Methylmethacrylates , Mice , Polyethylene Terephthalates , Polymethacrylic Acids , Species Specificity , StereoisomerismABSTRACT
Asparaginases from Escherichia coli and Erwinia caratovora were isolated and purified by column chromatography with a specific sorbent (sepharose, covalently bound to N-alpha-(6-aminohexyl)-D-asparagine). Homogenous asparaginase from E. coli was isolated by one-step procedure, while the enzyme from Er. carotovara was 50-60-fold purified. Asparaginase from Mycobacterium n. sp. was found not to bind with the specific sorbent.