پژوهه » دانلود رایگان مقالات لاتین در رشته زیست شناسی سلولی و مولکولی در موضوع cell membrane
دانلود رایگان مقالات لاتین در رشته زیست شناسی سلولی و مولکولی در موضوع cell membrane

دانلود رایگان مقالات لاتین در رشته زیست شناسی سلولی و مولکولی در موضوع cell membrane

 

Selective Solubilization of a Protein Component of the Red Cell Membrane

Abstract

Approximately 20 percent of the membrane-bound protein of erythrocyte ghosts can be solubilized and obtained free of other membrane components by dialysis against adenosine triphosphate and 2-mercaptoethanol. This protein forms one major band on polyacrylamide gels and a single boundary in free-boundary electrophoresis, and it undergoes polymerization in the presence of divalent cations to form coiled filaments visible by electron microscopy. Antibodies to this membrane protein react specifically with red blood cells or their membrane ghosts but do not react with serum, erythrocyte cytoplasm, or other blood cells. The functional role of this protein is unknown, but it appears to be involved in maintaiining the structure of the red cell membrane. We suggest that this protein be called Spectrin since it is obtained from membrane ghosts.

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TGF-bold beta signalling from cell membrane to nucleus through SMAD proteins

Carl-Henrik Heldin1, Kohei Miyazono2 & Peter ten Dijke1

The recent identification of the SMAD family of signal transducer proteins has unravelled the mechanisms by which transforming growth factor-beta (TGF-beta) signals from the cell membrane to the nucleus. Pathway-restricted SMADs are phosphorylated by specific cell-surface receptors that have serine/threonine kinase activity, then they oligomerize with the common mediator Smad4 and translocate to the nucleus where they direct transcription to effect the cell’s response to TGF-beta. Inhibitory SMADs have been identified that block the activation of these pathway-restricted SMADs.

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