By G. L. Nicolson (auth.), James K. Koehler Ph. D. (eds.)
The use of the time period "advanced" within the identify of this e-book is slightly ar bitrary and extremely a lot relative with recognize to time. Many recommendations which have been thought of on the "cutting side" of ultrastructural technique quite a few years in the past at the moment are rou tin ely utilized in a variety of laboratories. it is easy to cite freeze-fracture, cryothin sectioning, or certainly lots of the box of test ning electron microscopy as concrete examples. hence using the time period "ad vanced strategies" has to be interpreted with reference to the current state-of-the-art, and turns out to be useful merely in informing the capability reader that this quantity isn't a primer for use as an preliminary advent into uncomplicated organic elec tron microscopy. many glorious volumes have crammed that area of interest some time past few years, and it's not meant that this modest booklet be an entire com pendium of the sector. additionally, any constrained choice of papers on advanc ed thoughts unavoidably displays the personal tastes and arbitrary whims of the editor, thereby apart from many both very important approaches which the a professional reader will easily determine. the 1st quantity of this sequence seemed nearly 5 years in the past and illustrated ideas which have been concept to symbolize complex and but ba sically morphological equipment for gaining elevated ultrastructural informa tion from organic specimens. the current quantity, nonetheless, stresses ideas which offer particular physicochemical information at the speci mens as well as the structural information.
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Extra resources for Advanced Techniques in Biological Electron Microscopy II: Specific Ultrastructural Probes
Nature (New BioI) 244, 278 - 279 (1973) McFarlane, A. : Efficient trace-labelling of proteins with iodine. Nature (London) 182,53 (1958) Miller, J. , Kingdon, H. : Phytohemagglutinin mitogenic proteins. Structural evidence for a family of isomitogenic proteins. J. Exp. Med. 138,939 - 951 (1973) Miller, J. , Boyd, W. C: Immunochemical studies of lectins. I. Partial purification of the hemagglutinating protein of Sophora Japonica. Vox Sang. : Immunocyte triggering. Cell. Immunol. 1,573 - 582 (1970) Nicolson, G.
Science 184, 1294 -1296 (1974) Nicolson, G. ]. Cell BioI. : Lymphocyte transformation induced by concanavalin A and its reversion by methyl-alpha-D-mannopyranoside. Biochim. Biophys. , Barondes, S. : Agglutinin from Limulus polyphemus: purification with formalinized horse erythrocytes as the affinity adsorbent. Biochim. Biophys. Acta 393, 115 - 123 (1975) Oikawa, T, Nicolson, G. : Inhibition of hamster egg fertilization by phytoagglutinins. Exptl. Cell Res. , Nicolson, G. : Wheat germ agglutinin blocks mammalian fertilization.
Excess dextran-iron complex is removed by three washes as before, and the samples are postfixed in 1% osmium tetroxide in phosphate buffer for 1 h and dehydrated and embedded using standard procedures. The dextran-iron particles appear in a variety of sizes but are sufficiently electron dense to allow high resolution localization. The complex does not penetrate fixed cells, and controls without lectin are unlabeled, indicating absence of nonspecific binding to cell surfaces. 2. Lectin-Mannan-Iron Complexes ROTH and FRANZ (1975) utilized a purified yeast mannan to make mannan-iron complexes (see Sect.
Advanced Techniques in Biological Electron Microscopy II: Specific Ultrastructural Probes by G. L. Nicolson (auth.), James K. Koehler Ph. D. (eds.)