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Biblioteca(s):  Embrapa Florestas.
Data corrente:  25/09/2008
Data da última atualização:  25/09/2008
Autoria:  DICKOW, K. M. C.; ROCHA, A. A.; MAREQUES, R.; HOFER, H.; SCHEUERMANN, L.; ROMBKE, J.; FORSTER, B.; SCHMIDT, P.
Título:  Soil macrofauna contribution in decomposition processes of different plant species in the southern Mata Atlântica.
Ano de publicação:  2008
Fonte/Imprenta:  In: INTERNATIONAL COLLOQUIUM ON SOIL ZOOLOGY, 15; INTERNATIONAL COLLOQUIUM ON APTERYGOTA, 12., 2008, Curitiba. Biodiversity, conservation and sustainabele management of soil animal: abstracts. Colombo: Embrapa Florestas. Editors: George Gardner Brown; Klaus Dieter Sautter; Renato Marques; Amarildo Pasini. 1 CD-ROM.
Idioma:  Inglês
Conteúdo:  The contribution of soil fauna in decomposition processes of areas in the southern part of the Brazilian Mata Atlântica was studied in three different regeneration stages of lowland and submountain rainforests. Therefore abundance, biomass and structure of soil macrofauna communities was determined and the leaf decomposition rates of three plant species (Andira anthelminthica, Sloanea guianensis and Tibouchina pulchra) assessed by using three different mesh-sizes of litterbags (0.02, 0.5 mm and 4 mm). Decomposition of the three leaf species differed strongly. Tibouchina pulchra leaves disintegrated almost two times faster than the ones of Sloanea guianensis and about three times faster than Andira anthelminthica. Furthermore it was the only species were leaf decomposition was affected by soil fauna. Decomposition rates increased from the youngest to the oldest succession stage. All six sites were very much alike regarding the structure of their soil macro-arthropod communities. Ants strongly dominated in terms of abundance and biomass, but most are generalists or predators. They had a negative effect on decomposition rates, probably by influencing the decomposer community. Abundant decomposers were diplopods and in the older stages also termites. While beetles occur with high abundances in all sites, due to their minute size they were not important in terms of biomass. In this regard cockroaches, diplopods and isopods were most important. Concerning the abundance or biomass ... Mostrar Tudo
Categoria do assunto:  --
Marc:  Mostrar Marc Completo
Registro original:  Embrapa Florestas (CNPF)
Biblioteca ID Origem Tipo/Formato Classificação Cutter Registro Volume Status URL
CNPF43722 - 1UPEPL - --CD0305
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Biblioteca(s):  Embrapa Recursos Genéticos e Biotecnologia.
Data corrente:  15/02/2005
Data da última atualização:  29/05/2018
Autoria:  TIROLI, A. O.; TASIC, L.; OLIVEIRA, C. L. P.; BLOCH JUNIOR, C.; TORRIANI, I.; FARAH, C. S.; RAMOS, C. H. I.
Título:  Mapping contacts between regulatory domains of skeletal muscle TnC and Tnl by analyses of a single-chain chimeras.
Ano de publicação:  2005
Fonte/Imprenta:  The FEBS Journal, v. 272, n. 2, p. 779-790, 2005.
Idioma:  Inglês
Conteúdo:  The troponin (Tn) complex is formed by TnC, TnI and TnT and is responsible for the calcium-dependent inhibition of muscle contraction. TnC and TnI interact in an antiparallel fashion in which the N domain of TnC binds in a calcium-dependent manner to the C domain of TnI, releasing the inhibitory effect of the latter on the actomyosin interaction. While the crystal structure of the core cardiac muscle troponin complex has been determined, very little high resolution information is available regarding the skeletal muscle TnITnC complex. With the aim of obtaining structural information regarding specific contacts between skeletal muscle TnC and TnI regulatory domains, we have constructed two recombinant chimeric proteins composed of the residues 191 of TnC linked to residues 98182 or 98147 of TnI. The polypeptides were capable of binding to the thin filament in a calcium-dependent manner and to regulate the ATPase reaction of actomyosin. Small angle X-ray scattering results showed that these chimeras fold into compact structures in which the inhibitory plus the C domain of TnI, with the exception of residues 148182, were in close contact with the N-terminal domain of TnC. CD and fluorescence analysis were consistent with the view that the last residues of TnI (148182) are not well folded in the complex. MS analysis of fragments produced by limited trypsinolysis showed that the whole TnC N domain was resistant to proteolysis, both in the presence and in the absence of calcium. O... Mostrar Tudo
Palavras-Chave:  Muscle.
Categoria do assunto:  --
URL:  https://ainfo.cnptia.embrapa.br/digital/bitstream/item/177877/1/ID-24788.pdf
Marc:  Mostrar Marc Completo
Registro original:  Embrapa Recursos Genéticos e Biotecnologia (CENARGEN)
Biblioteca ID Origem Tipo/Formato Classificação Cutter Registro Volume Status
CENARGEN24788 - 1UPCAP - DDSP 1836918369
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