Diagnóstico ambiental de uma nascente na cabeceira de drenagem do Rio Tibagi, Municipio de Ponta Grossa: análise preliminar.

A área de estudo encontra - se no município de Ponta Grossa, e compreende um campo hidrófilo de altitude que abriga uma das nascente do rio Caracará , afluente da margem direita do r io Tibagi . Com objetivo de caracterizar a qualidade das águas d esta nascente foi realizado campanhas de campo para a realização de uma caracterização hidroquímica preliminar. Os parâmetros avaliados foram Ca 2+ , Mg 2+ , Na + , K+, Cl - , HCO 3 - e SO 4= , compostos nitrogenados, NH 3 e NO 3 - , dureza, Fe; pH e CE . Neste estudo foram analisados 9 pontos amostrais distribuídos em triplicata , sendo 3 pontos de coleta instalados em cada faixa de declive representativa na nascente . A caracterização hidroquímica preliminar foi elaborada com base n a Portaria n° 2914 /2011 e n a Resolução C ONAMA n° 357/2005 e 396/2008 . O resultados preliminares indicaram que a nascente do rio Caracará localizada no campo hidrófilo de altitude apresentou teores de fósforo (0,0 4 mg/L) acima dos valores máximos permitidos para ambientes lêntico s. A s águas forma classificadas como bicabornatadas cálcicas ou magnesianas . Este monitoramento preliminar reuniu informações para dar aporte a proteção das nascentes e propiciar um melhor planejamento do manejo das águas superficiais no município de Ponta Grossa e d a bacia do rio Tibagi no estado do Paraná

A postsynaptic Mr 58,000 (58K) protein concentrated at acetylcholine receptor-rich sites in Torpedo electroplaques and skeletal muscle

In the study of proteins that may participate in the events responsible for organization of macromolecules in the postsynaptic membrane, we have used a mAb to an Mr 58,000 protein (58K protein) found in purified acetylcholine receptor (AChR)-enriched membranes from Torpedo electrocytes. Immunogold labeling with the mAb shows that the 58K protein is located on the cytoplasmic side of Torpedo postsynaptic membranes and is most concentrated near the crests of the postjunctional folds, i.e., at sites of high AChR concentration. The mAb also recognizes a skeletal muscle protein with biochemical characteristics very similar to the electrocyte 58K protein. In immunofluorescence experiments on adult mammalian skeletal muscle, the 58K protein mAb labels endplates very intensely, but staining of extrasynaptic membrane is also seen. Endplate staining is not due entirely to membrane infoldings since a similar pattern is seen in neonatal rat diaphragm in which postjunctional folds are shallow and rudimentary, and in chicken muscle, which lacks folds entirely. Furthermore, clusters of AChR that occur spontaneously on cultured Xenopus myotomal cells and mouse muscle cells of the C2 line are also stained more intensely than the surrounding membrane with the 58K mAb. Denervation of adult rat diaphragm muscle for relatively long times causes a dramatic decrease in the endplate staining intensity. Thus, the concentration of this evolutionarily conserved protein at postsynaptic sites may be regulated by innervation or by muscle activity

Ultrastructural localization of the Mr 43,000 protein and the acetylcholine receptor in Torpedo postsynaptic membranes using monoclonal antibodies

Four mouse monoclonal antibodies (mabs) were shown by immunoblotting procedures to recognize the major, basic, membrane-bound Mr 43,000 protein (43K protein) of acetylcholine receptor-rich postsynaptic membranes from Torpedo nobiliana . These mabs and a mab against an extracellular determinant on the acetylcholine receptor were used to localize the two proteins in electroplax (Torpedo californica) and on unsealed postsynaptic membrane fragments at the ultrastructural level. Bound mabs were revealed with a rabbit anti-mouse Ig serum and protein A-colloidal gold. The anti-43K mabs bound only to the cytoplasmic surface of the postsynaptic membrane. The distributions of the receptor and the 43K protein along the membrane were found to be coextensive. Distances between the membrane center and gold particles were very similar for anti-receptor and anti-43K mabs (29 +/- 7 nm and 26 to 29 +/- 7 to 10 nm, respectively). These results show that the 43K protein is a receptor-specific protein having a restricted spatial relationship to the membrane. They thus support models in which the 43K protein is associated with the cytoplasmic domains of the receptor molecule

Guia prático para preparação de amostras sedimentares para a análise de ácidos biliares e esteróis fecais por cromatografia gasosa - espectrometria de massa (GC-MS).

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