RESUMO
Quinolinic acid was administered intraperitoneally in a dose of 30 or 60 mmol, once every 24 h for 8 days. Its result in the dose of 30 mmol was the proliferation of smooth elements of the endoplasmic reticulum. The use of quinolinic acid in a dose of 60 mmol was characterized by the presence of more profound damage of organelles, among them the distinct decrease of the rough elements of the endoplasmic reticulum and polyribosomal structures was seen, and moreover, wide areas devoid of organelles were observed.
Assuntos
Fígado/efeitos dos fármacos , Fígado/ultraestrutura , Ácido Quinolínico/farmacologia , Animais , Relação Dose-Resposta a Droga , Injeções Intraperitoneais , Masculino , Ácido Quinolínico/administração & dosagem , Ratos , Ratos WistarRESUMO
The main forms of arginase A1 from human kidney and A5 from human liver were purified to homogeneity. Molecular weight of both forms of enzyme approximates 120,000. In the presence of EDTA these arginases dissociate into single type distinct subunits. M(r) of both kinds of subunits is 30,000. Similarly as native arginase forms, they differ in electric charge and display complete immunological incompatibility.
Assuntos
Arginase/química , Rim/enzimologia , Fígado/enzimologia , Adulto , Arginase/imunologia , Arginase/isolamento & purificação , Ácido Edético , Eletroforese em Gel de Poliacrilamida , Humanos , Imunodifusão , Imunoeletroforese , Pessoa de Meia-Idade , Peso Molecular , Conformação Proteica , Distribuição TecidualRESUMO
Five forms of arginase, A1, A2, A3, A4, and A5, were found to be present in human tissues. The molecular weight of all these forms is the same, 120,000, but they differ in the behavior on DEAE- and CM-cellulose, electrophoretic mobility, isoelectric point, and immunochemical properties. Forms A1 from kidney and A5 from liver show complete immunological incompatibility, whereas forms A2 from liver, A3 from salivary gland, and A4 from kidney exhibit partial incompatibility with respect to each other and to forms A1 and A5.
Assuntos
Arginase/isolamento & purificação , Isoenzimas/isolamento & purificação , Rim/enzimologia , Fígado/enzimologia , Glândula Submandibular/enzimologia , Adulto , Cromatografia por Troca Iônica , Reações Cruzadas , Humanos , Soros Imunes , Imunoeletroforese , Focalização Isoelétrica , Peso Molecular , Especificidade de ÓrgãosRESUMO
1. Two forms of arginase were isolated from human erythrocytes; the main form adsorbed on CM-cellulose and the second form, occurring in much smaller amount, adsorbed on DEAE-cellulose. 2. The molecular weight of either arginase was 120,000 +/- 5000. 3. The erythrocyte arginases are similar in immunological properties to arginase A4 from human kidney and A2 from human liver, respectively. 4. Despite the literature data stating that human erythrocyte arginase and human liver arginase are identical, it was found that the main forms of arginase of these tissues A4 from erythrocytes and A5 from liver differ in immunological properties.
Assuntos
Arginase/sangue , Eritrócitos/enzimologia , Arginase/imunologia , Arginase/isolamento & purificação , Cromatografia por Troca Iônica , Reações Cruzadas , Humanos , Soros Imunes , Imunodifusão , Imunoeletroforese , Rim/enzimologia , Cinética , Fígado/enzimologia , Peso MolecularRESUMO
Five immunologically different forms of arginase were evidenced in rat tissues by the double diffusion test and immunoelectrophoresis. New symbols for these arginases are proposed (beginning with the most anionic forms): A1 (kidney), A2 (liver), A3 (salivary glands), A4 (kidney) and A5 (liver). Arginases A1 from kidney and A5 from liver are paternal forms built of one-type subunits. Subunits of form A1 exhibit a non-identity cross-reaction with subunits of form A5. Arginases A2, A3 and A4 are hybrids composed of both kinds of subunits.
