Advanced Techniques in Biological Electron Microscopy II: by G. L. Nicolson (auth.), James K. Koehler Ph. D. (eds.)

By G. L. Nicolson (auth.), James K. Koehler Ph. D. (eds.)

The use of the time period "advanced" within the name of this e-book is a little ar­ bitrary and extremely a lot relative with admire to time. Many suggestions that have been thought of on the "cutting area" of ultrastructural method quite a few years in the past at the moment are rou tin ely utilized in a number of laboratories. you will cite freeze-fracture, cryothin sectioning, or certainly many of the box of test­ ning electron microscopy as concrete examples. therefore using the time period "ad­ vanced suggestions" has to be interpreted with reference to the current cutting-edge, and comes in handy purely in informing the capability reader that this quantity isn't a primer for use as an preliminary creation into simple organic elec­ tron microscopy. many fantastic volumes have crammed that area of interest long ago few years, and it isn't meant that this modest e-book be an entire com­ pendium of the sphere. in addition, any restricted number of papers on advanc­ ed strategies inevitably displays the personal tastes and arbitrary whims of the editor, thereby except for many both vital techniques which the an expert reader will with no trouble establish. the 1st quantity of this sequence seemed nearly 5 years in the past and illustrated concepts which have been concept to symbolize complex and but ba­ sically morphological tools for gaining elevated ultrastructural informa­ tion from organic specimens. the current quantity, nevertheless, stresses recommendations which supply particular physicochemical info at the speci­ mens as well as the structural information.

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J. Ultrastruct. Res. : Temperature effects on concanavalin A molecule and on concanavalin A binding. Biochim. Biophys. : Interactions entre la concanavaline A et ses recepteurs a la surface cellulaire: Etude ultrastructurale. T. Micros. BioI. Cell. : Inhibition of ascites tumor development by concanavalin A. Int. J. , Huet, C, Oseroff, A. : Inhibition of lectin agglutinability by fixation of the cell surface membrane. Biochim. Biophys. : Further studies on the specificity of the anti-A agglutinin from Helix pomatia.

The cells are rinsed twice in media and postfixed in 2% osmium tetroxide in the phosphate buffer, dehydrated, and embedded in Araldite, "Epon" 812 or Spurr resin. Sections can be examined unstained or they can be counterstained briefly (2 - 5 min) with lead citrate. The main advantages of the two-step lectin-peroxidase method are that it is uncomplicated, reliable, and labeling reagents do not have to be purified beyond that of commercial preparations. In addition, native unmodified lectin is used for the labeling experiments as opposed to lectin conjugates.

1974) HUET and BERNADAC (1974) Efficiency of peroxidase labeling Temperature effects on lectin HUETetal. (1974) binding and redistribution Normal liver and hepatoma cells ROTH (1974) ACKERMAN and WAKSAL(1974) Human bone marrow cells Ehrlich ascites cells ROTH and THOSS (1974) GORDON et al. (1974) Rabbit sperm Erythrocytes and tumor cells ROTH et al. (1975) Endocytosis and dynamics on normal HUET and BERNADAC and transformed cells (1975) ROTH (1975 a) Mouse lung cells Con A Con A Con A Con A WGA WGA, Con A Con A Con A Con A Con A WGA,ConA, RCA LCA, Con A Con A Con A WGA, Con A Con A Con A Con A Con A Con A LCA Con A LCA Con A Con A, RCA, LCA Con A LCA Con A Con A, WGA Normal and transformed cells Normal and transformed rat liver cells Normal and transformed rat liver cells Hamster cells at various cell cycle stages Reference COLLARD et al.

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