RESUMEN
Glycoprotein such as neuraminidase is an enzyme occurring in some viruses and bacteria. It is characterized by a series of specific biochemical, enzymatic and immunological properties. The observed prevalence of chronic virus infections as well as liver diseases, glomerulonephritis, conjunctive tissue diseases and other autoaggressive illnesses which occur in their course have become the reason for experimental studies in which according to established patterns enzymatically active and inactive neuraminidase was administered to rabbits in a prolonged way.
Asunto(s)
Neuraminidasa/fisiología , Animales , Bacterias/enzimología , Infecciones Bacterianas/enzimología , Humanos , Neuraminidasa/química , Conejos , Virosis/enzimología , Virus/enzimologíaRESUMEN
Corticostriate projections from the hindlimb and forelimb areas of the primary motor cortex in the dog were traced using the autoradiographic technique. Injections of tritiated leucine into the hindlimb area resulted in discrete oval or semicircular patches of label confined to the dorsolateral corner of the head and body of the caudate nucleus. No label was found over the putamen. Injections into the forelimb area yielded irregularly shaped patches of label over the dorsolateral part of the head and body of the caudate nucleus as well as more diffuse label over the dorsal-most part of the putamen. In both instances diffuse terminal fields were noted in the dorsolateral part of the contralateral caudate nucleus. A comparison of results in the caudate nucleus indicates that projections from the forelimb area terminate somewhat more caudally and slightly more ventrally and medially than do projections from the hindlimb area. The results further suggest that although terminal fields from these areas may to some extent interdigitate with one another, they also overlap each other to a significant degree.
Asunto(s)
Cuerpo Estriado/anatomía & histología , Corteza Motora/anatomía & histología , Animales , Autorradiografía , Núcleo Caudado/anatomía & histología , Perros , Miembro Anterior/inervación , Miembro Posterior/inervación , Vías Nerviosas/anatomía & histología , Neuronas/ultraestructura , Putamen/anatomía & histologíaRESUMEN
Specifically purified anti-TNP antibodies of subclass IgGI and IgG2 were isolated using immunoadsorbent prepared from AH-Sepharose and TNP-BSA. Isoelectric focusing in poliacrylamide gel showed differences between antibodies obtained from colostrum and serum. These differences were more observable when H chains of IgG1 subclasses were compared. No differences were observed in L chains. The antibodies obtained were the non-precipitating ones. Spectral measurements in the presence of SO3- ions, showed that the antibodies studied were of low affinity (below 10(-6) M). The difference spectra showed, that binding of a hapten (epsilon-TNP aminocapronate acid) to the investigated antibodies caused the shift of the hapten's absorption bands indicating that the binding occured in the hydrophobic pocket of the antibody binding site. The strongest effect was observed in the case of antibodies of IgG1 subclass.
Asunto(s)
Especificidad de Anticuerpos , Calostro/inmunología , Inmunoglobulina G , Nitrobencenos/inmunología , Trinitrobencenos/inmunología , Animales , Bovinos , Femenino , Punto Isoeléctrico , Lactancia , Embarazo , Análisis Espectral , Factores de TiempoRESUMEN
Human secretory IgA was prepared from colostrum. Different elution diagrams from CM-cellulose were obtained depending on the time of collection of colostrum. In case of early colostrum, collected within 6 hours post partum, two IgA fractions were obtained after chromatography on CM-cellulose. Both fractions have different molecular weights and different amino acid compositions. The results obtained suggest that the first fraction is a dimer of IgA monomers containing J chain with a molecular weight of 330,000 whereas the second fraction having the molecular weight 395,000 daltons is composed of IgA dimer, J chain and SC. When colostrum collected 48 or more hours was used as a source of IgA, only the second IgA fraction was obtained. The problem of SC-free IgA immunoglobulins is discussed.