RESUMEN
The activities of protein kinase C, total, Mg2 and Na+, K(+)-dependent ATPases in red cell membranes were compared in 46 patients with insulin independent, 30 ones with insulin dependent diabetes mellitus with various degrees of vascular disorders, and in 17 patients with atherosclerosis with the predominant involvement of the main vessels of the lower limbs. Diabetes mellitus and the progress of vascular disorders were associated with a more marked depression of protein kinase C, total and Na+, K(+)-dependent ATPase activities, this being particularly characteristic of the patients with insulin-independent diabetes and macrovascular disorders. Inhibited activities of protein kinase C and ATPases in red cell membranes in the course of diabetic vascular disorders progress evidence their contribution to the pathogenesis of diabetic angiopathy.
Asunto(s)
Adenosina Trifosfatasas/sangre , Arteriosclerosis/enzimología , Angiopatías Diabéticas/enzimología , Membrana Eritrocítica/enzimología , Proteína Quinasa C/sangre , ATPasa Intercambiadora de Sodio-Potasio/sangre , Adolescente , Adulto , Anciano , Arteriosclerosis/sangre , Angiopatías Diabéticas/sangre , Femenino , Humanos , Masculino , Persona de Mediana EdadRESUMEN
Data are presented on the level of stable metabolites of prostacyclin I2-thromboxane A2 system in streptozotocin diabetes mellitus in rats. It is shown that simulation of streptozotocin diabetes mellitus leads to the reduction of 6-ketoprostaglandin F1 alpha content in the aortal wall tissue and blood plasma, and to a rise of thromboxane B2 level and the thromboxane B2/6-ketoprostaglandin F1 alpha ratio in the blood plasma. Inclusion of docosahexaenic and eicosapentaenic acid concentrate into the ration of animals with streptozotocin diabetes mellitus is conducive to normalization of the stable metabolite level in the prostacyclin I2-thromboxane A2 system.
Asunto(s)
Diabetes Mellitus Experimental/metabolismo , Ácidos Docosahexaenoicos/farmacología , Ácido Eicosapentaenoico/farmacología , Epoprostenol/metabolismo , Tromboxano A2/metabolismo , 6-Cetoprostaglandina F1 alfa/sangre , 6-Cetoprostaglandina F1 alfa/metabolismo , Animales , Aorta/metabolismo , Diabetes Mellitus Experimental/sangre , Masculino , Ratas , Tromboxano B2/sangreRESUMEN
13 peptic peptides have been isolated from the insoluble (at pH 5.0) fraction of the tryptic hydrolysate of main chromatographic component of otter myoglobin and their amino acid composition and N-terminal amino acid sequences have been determined. The isolated peptides contain in total 40 amino acid residues. The results obtained, along with those on tryptic peptides and the comparison with homologous portions of myoglobins of the known primary structure, allowed reconstructing the complete amino acid sequence of otter myoglobin.
Asunto(s)
Carnívoros , Globinas/análisis , Mioglobina/análisis , Nutrias , Péptidos/análisis , Secuencia de Aminoácidos , Animales , Hidrólisis , TripsinaRESUMEN
The amino acid sequence of 24 soluble tryptic peptides has been determined for the main chromatographic component of otter myoglobin. Fractionation, identification and peptide isolation have been made by fingerprints. The isolated peptides contain in total 111 amino acid residues.