Fine structure of bone resorption in experimental osteoporosis caused by calcium deficient diet in rats. An electron microscopic study of compact bone

1970 ◽  
Vol 4 (1) ◽  
pp. 80-82 ◽  
Author(s):  
C. D. Salomon ◽  
G. Volpin
Keyword(s):  
Fine Structure ◽  
Bone Resorption ◽  
Microscopic Study ◽  
Electron Microscopic Study ◽  
Compact Bone ◽  
Electron Microscopic ◽  
Deficient Diet ◽  
Experimental Osteoporosis

An electron microscopic study of Amoeba proteus

1959 ◽  
Vol 150 (939) ◽  
pp. 216-232 ◽  
Keyword(s):  
Electron Microscopy ◽  
Fine Structure ◽  
Microscopic Study ◽  
Electron Microscopic Study ◽  
Amoeba Proteus ◽  
Contractile Vacuole ◽  
Electron Microscopic ◽  
Functional Implications ◽  
Food Vacuoles

Methods of fixing, embedding and sectioning of Amoeba proteus for electron microscopy are described. The fine structure of the various organelles: nucleus, mitochondria, food vacuoles; and the contractile vacuole, is discussed in detail. A number of minor unidentified objects has also been found. The functional implications of the structural findings are considered.

An electron-microscopic study of Herpetomonas sp. (Leptomonas pessoai)

1976 ◽  
Vol 22 (2) ◽  
pp. 197-203 ◽  
Author(s):  
Wanderley De Souza ◽  
M. A. Rossi ◽  
E. W. Kitajima ◽  
R. R. Santos ◽  
I. Roitman
Keyword(s):  
Fine Structure ◽  
Microscopic Study ◽  
Electron Microscopic Study ◽  
Defined Medium ◽  
Particulate Material ◽  
Large Cavity ◽  
Electron Microscopic ◽  
Crithidia Fasciculata

The fine structure of the promastigotes of Herpetomonas sp. (Leptomonas pessoai) kept in a defined medium at 28 °C is described. This protozoon reveals several features in common with other trypanosomatids. A membrane-bounded organelle measuring 0.2 to 0.8 μm in diameter, similar to that described as peroxisome in Crithidia fasciculata, was also observed. A large cavity, located between the nucleus and the kinetoplast and containing vesicles and small particulate material is discussed in this paper.

Fine structure of the human coccygeal body: a light and electron microscopic study

1998 ◽  
Vol 180 (1) ◽  
pp. 11-14 ◽  
Author(s):  
Mustafa F. Sargon ◽  
H. Hamdi Çelik ◽  
Deniz Demiryürek ◽  
Atilla Dağdeviren
Keyword(s):  
Fine Structure ◽  
Microscopic Study ◽  
Electron Microscopic Study ◽  
Electron Microscopic

scholarly journals The effect of EDTA, cations, and various buffers on the morphology of erythrocyte membranes: an electron-microscopic study

Blood ◽  
1975 ◽  
Vol 45 (5) ◽  
pp. 709-724 ◽  
Author(s):  
L Pinteric ◽  
JF Manery ◽  
IH Chaudry ◽  
G Madapallimattam
Keyword(s):  
Fine Structure ◽  
Electron Microscope ◽  
Microscopic Study ◽  
Electron Microscopic Study ◽  
Ethylenediaminetetraacetic Acid ◽  
Human Erythrocytes ◽  
Erythrocyte Membranes ◽  
Electron Microscopic ◽  
Osmotic Hemolysis ◽  
Ionic Calcium

Abstract Membranes of human erythrocytes were prepared by stepwise osmotic hemolysis in Ca2+-free solutions. Examination with the electron microscope after negative staining showed some short, conelike protuberances on the surface of about 20 percent of the ghosts, while 80 percent were round, intact spheres. After Ca2+ treatment, all membranes were round and intact. After exposure to ethylenediaminetetraacetic acid (EDTA) (1.0 mM, pH 7.4), the entire ghost surface was covered with long, thin extrusions called stromalytic forms (about 460 per cell). Their sizes, shapes, and fine structure are described. Exposure to ionic calcium (1.4 times 10-minus 4M) abolished the EDTA-induced stromalytic forms. A second exposure to EDTA reversed this Ca2+ effect. ATP, like EDTA, produced stromalytic forms. EDTA- induced stromalytic forms were also abolished by Zn2+, La3+, and Nd3+ at concentrations of 1–5 times 10-minus 4 M. Mg2+ at 10-minus 2 M was ineffective. Ghosts were prepared by graded lysis in various buffers. Those prepared in phosphate were the most stable and provided consistent EDTA effects and Ca2+ reversal. Ghosts in Tris-HCl showed breakdown unless salt was added. Moderately satisfactory ghosts were also obtained in Hepes-NaOH buffer and salt.

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