Immuno-electron microscopy

Bendayan, M. (1989) Protein A-gold and protein G-gold postembedding immuno-electron microscopy, in Colloidal Gold, vol. 1 (Hayat, M. A., ed.). Academic, New York, pp. 34-96. 

DNA, since proximity eflfects demand that the DNA or nascent RNA closest to the histones at the point of disruption will be the polyanion for which those histones will preferentially reassociate. Ten Heggeler-Bordier et al. [95] have verified these observations. They used immuno-electron microscopy to determine what happens to histones after transcription with T7 RNA polymerase of a multi-nucleosomal template and also observed transfer to the nascent RNA. In contrast, Kirov et al. [96] have reported that no histones displace during transcription with this polymerase. However, as described above, transcriptional efficiency and ultimately histone displacement is not efficient in very low ionic strength conditions. 

Fig. 18 Immuno-electron microscopy showing detection of malic enzyme in the hydro-genosomes (H) of T. vaginalis. N, nucleus bar = 100 nm. (Benchimol, unpublished)...

Because of the high specificity of an antibody for its epitope, an antibody raised against a particular protein antigen can be used to determine the location of that antigen in a cell using immunofluorescence light microscopy or immuno-electron microscopy. 

Gerhmann, J., Bonnekoh, P., Miyazawa, T., Oschlies, U., Dux, E., Hossman, K.-A., and Kreutzberg, G. W., The microglial reaction in the rat hippocampus following global ischaemia immuno-electron microscopy, Acta Neuropathol., 84, 588, 1992. 

Nixon, R. A., Wegiel, J., Kumar, A., Yu, W. H., Peterhoff, C., Cataldo, A., and Cuervo, A. M., Extensive involvement of autophagy in Alzheimer disease an immuno-electron microscopy study, J Neuropathol Exp Neurol 64 (2005) 113-122. 

Several experiments have indicated that the ER is the site of addition of the bulk of TG to apo B. First, the size distribution of lipoproteins is the same in the lumen of the ER and Golgi of rat liver, and in newly secreted lipoproteins (J.E. Vance, 1993). Furthermore, a series of pulse-chase radiolabeling experiments in rat hepatoma cells indicate that the majority of TG associates with apo B in the ER (H.N. Ginsberg, 2003). On the other hand, immuno-electron microscopy studies in rat liver (R.J. Havel, 1976), and pulse-chase radiolabeling experiments in chicken hepatocytes (M.D. Lane, 1990) and rat hepatoma cells (E.A. Fisher, 2003), have suggested that the majority of TG assembles with apo B in the Golgi apparatus. The reasons for these conflicting conclusions remain unclear. 

In S-IBM muscle fibers, our studies have demonstrated proteasomal abnormalities, as evidenced by (a) abnormal accumulation of 26S proteasome subunits by immunocytochemistry and immuno-electron microscopy (b) increased expression of 26S proteasome subunits by immunoblots but, contrastingly (c) reduced activities of the three major proteasomal proteolytic enzymes [11]. This indicates accumulation of hypo-active/inactive proteasomal subunit proteins. 

Figure 7.3 Single-label gold-immuno-electron microscopy of Ap42, and double-label gold immuno-electron microscopy of p62 plus p-tau in s-IBM muscle fibers. (a)A)S42 (Snmgoldparticles) is immunolocalizedto 6-10 nm amyloid-like fibrils, while in (b) p62 (lOnmgold particles) and p-tau (5 nm gold particles) intermingle on paired-helical filaments. Magnification (a) xSO.OOO ...

By immuno-electron microscopy, CD8 cells and macrophages send spike-hke processes into notme-crotic muscle fibers, which traverse the basal lamina and locally displace or compress the muscle fibers [18]. 

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