scholarly journals Location of peptide fragments in the fibrinogen molecule by immunoelectron microscopy.

1980 ◽  
Vol 77 (5) ◽  
pp. 2372-2376 ◽  
Author(s):  
J. N. Telford ◽  
J. A. Nagy ◽  
P. A. Hatcher ◽  
H. A. Scheraga
Keyword(s):  
Immunoelectron Microscopy ◽  
Peptide Fragments ◽  
Fibrinogen Molecule

Ultrastructural investigation of spontaneous pituitary gonadotroph cell adenomas in aging Sprague-Dawley rats

1983 ◽  
Vol 41 ◽  
pp. 702-703
Author(s):  
D. J. McComb ◽  
J. Beri ◽  
F. Zak ◽  
K. Kovacs
Keyword(s):  
Electron Microscopy ◽  
Animal Model ◽  
Epoxy Resin ◽  
Immunoelectron Microscopy ◽  
Tumor Type ◽  
Gonadal Function ◽  
Sprague Dawley ◽  
Male And Female ◽  
Reticulin Fibers ◽  
Sprague Dawley Rats

Gonadotroph cell adenomas of the pituitary are infrequent in human patients and are not invariably associated with altered gonadal function. To date, no animal model of this tumor type exists. Herein, we describe spontaneous gonadotroph cell adenomas in old male and female Sprague-Dawley rats by histology, immunocytology and electron microscopy.The material consisted of the pituitaries of 27 male and 38 female Sprague Dawley rats, all 26 months of age or older, removed at routine autopsy. Sections of formal in-fixed, paraffin-embedded tissue were stained with hematoxylin-phloxine-saffron (HPS), the PAS method and the Gordon-Sweet technique for the demonstration of reticulin fibers. For immunostaining, sections were exposed to anti-rat β-LH, anti-ratβ-TSH, anti-rat PRL, anti-rat GH and anti-rat ACTH 1-39. For electron microscopy, tissue was fixed in 2.5% glutaraldehyde, postfixed in 1% OsO4 and embedded in epoxy-resin. Tissue fixed in 10% formalin, embedded in epoxy resin without osmification, was used for immunoelectron microscopy.

Solid-phase immunoelectron microscopy for rapid diagnosis of enteroviruses

1984 ◽  
Vol 42 ◽  
pp. 226-227 ◽  
Author(s):  
K. Pegg-Feige ◽  
F. W. Doane
Keyword(s):  
Electron Microscopy ◽  
Cell Culture ◽  
Immunoelectron Microscopy ◽  
Detection Method ◽  
Solid Phase ◽  
Protein A ◽  
Plant Viruses ◽  
Rapid Diagnosis ◽  
Virus Diagnosis ◽  
Antiviral Antibody

Immunoelectron microscopy (IEM) applied to rapid virus diagnosis offers a more sensitive detection method than direct electron microscopy (DEM), and can also be used to serotype viruses. One of several IEM techniques is that introduced by Derrick in 1972, in which antiviral antibody is attached to the support film of an EM specimen grid. Originally developed for plant viruses, it has recently been applied to several animal viruses, especially rotaviruses. We have investigated the use of this solid phase IEM technique (SPIEM) in detecting and identifying enteroviruses (in the form of crude cell culture isolates), and have compared it with a modified “SPIEM-SPA” method in which grids are coated with protein A from Staphylococcus aureus prior to exposure to antiserum.

Detection of Viral Antigens in Mouse and Rat Tumor Cells by Immunoelectron Microscopy Following Periodate-Lysine-Paraformaldehyde (PLP) Fixation

1976 ◽  
Vol 34 ◽  
pp. 252-253
Author(s):  
Y. Ohtsuki ◽  
G. Seman ◽  
J. M. Bowen ◽  
M. Scanlon ◽  
L. Dmochowski
Keyword(s):  
Immunoelectron Microscopy ◽  
Mammary Tumor ◽  
Type A ◽  
Rabbit Serum ◽  
Virus Particles ◽  
Viral Antigens ◽  
Culture Cells ◽  
Mouse Mammary Tumor ◽  
Tumor Virus ◽  
Immunoperoxidase Labeling

Recently, periodate-lysine-paraformaldehyde (PLP) fixation was reported for immunoelectron microscopy (1). In PLP fixation, carbohydrates are oxidized by periodate and cross-linked by lysine; paraformaldehyde stabilizes proteins and lipids. By using PLP fixation, intracytoplasmic type A viral antigens have been previously demonstrated by immunoperoxidase labeling (2). In the present study, PLP fixation has been applied for the detection of the same antigens in mouse mammary tumor culture cells by both immunoferritin and immunoperoxidase methods. Rabbit anti-intracytoplasmic type A virus serum (anti-A), kindly provided by Dr. M. Muller (3), rabbit anti-strain A mouse mammary tumor virus (anti-MMTV) and preimmune rabbit serum as control were used to detect viral antigens in cells of C3H/HeJ strain mouse mammary tumor culture. Attempts have been also made to demonstrate peroxidase labeling of type C virus particles in frozen sections of an SD-MSV-induced NZB rat bone tumor tissue by rabbit anti-MuLV serum.

Identification of maize mosaic virus by immunoelectron microscopy

1986 ◽  
Vol 44 ◽  
pp. 240-241
Author(s):  
O. E. Bradfute
Keyword(s):  
Zea Mays ◽  
Mosaic Virus ◽  
Immunoelectron Microscopy ◽  
Severe Disease ◽  
Maize Mosaic Virus ◽  
The World ◽  
Plant Rhabdovirus

Maize mosaic virus (MMV) causes a severe disease of Zea mays in many tropical and subtropical regions of the world, including the southern U.S. (1-3). Fig. 1 shows internal cross striations of helical nucleoprotein and bounding membrane with surface projections typical of many plant rhabdovirus particles including MMV (3). Immunoelectron microscopy (IEM) was investigated as a method for identifying MMV. Antiserum to MMV was supplied by Ramon Lastra (Instituto Venezolano de Investigaciones Cientificas, Caracas, Venezuela).

Banded aggregates containing fibrillin are present in the cartilage matrix adjacent to chondrocytes in individuals affected with scoliosis

1992 ◽  
Vol 50 (1) ◽  
pp. 892-893
Author(s):  
Douglas R. Keene ◽  
Magaret Fairhurst ◽  
Catherine C. Ridgway ◽  
Lynn Y. Sakai
Keyword(s):  
Connective Tissue ◽  
Marfan Syndrome ◽  
Cross Section ◽  
Immunoelectron Microscopy ◽  
Cartilage Matrix ◽  
Negative Stain ◽  
Gene Coding ◽  
Rotary Shadowing

Matrix microfibrils are present in the connective tissue matrices of all tissues. Following standard TEM processing, they appear in cross section as cylindrical fibrils 8-10 nm in diameter, often associated with amorphous elastin. They are also seen in the absence of amorphous elastin, for example in the shallow papillary layer of skin, and also in cartilage matrix (Figure 1). Negative stain and rotary shadowing studies suggest that microfibrils are composed of laterally associated globular structures connected by fine filamentous strands (“ beaded strings”), and that they are extendable. Immunoelectron microscopy has demonstrated that fibrillin, a 350 Kd glycoprotein, is distributed along all microfibrils with a relaxed periodicity of about 54 nm The gene coding for fibrillin has recently been identified and is defective in the Marfan syndrome.

Immunocytochemical studies on the behavior of RuBisCO and LHCP II during the cell cycle of synchronized Euglena gracilis

1990 ◽  
Vol 48 (3) ◽  
pp. 662-663
Author(s):  
Tetsuaki Osafune ◽  
Shuji Sumida ◽  
Tomoko Ehara ◽  
Eiji Hase ◽  
Jerome A. Schiff
Keyword(s):  
Cell Cycle ◽  
Immunoelectron Microscopy ◽  
Growth Phase ◽  
Euglena Gracilis ◽  
Dark Period ◽  
Light Period ◽  
Carboxylase Activity ◽  
Immunocytochemical Studies ◽  
Lhcp Ii

Changes in the morphology of pyrenoid and the distribution of RuBisCO in the chloroplast of Euglena gracilis were followed by immunoelectron microscopy during the cell cycle in a light (14 h)- dark (10 h) synchronized culture under photoautotrophic conditions. The imrnunoreactive proteins wereconcentrated in the pyrenoid, and less densely distributed in the stroma during the light period (growth phase, Fig. 1-2), but the pyrenoid disappeared during the dark period (division phase), and RuBisCO was dispersed throughout the stroma. Toward the end of the division phase, the pyrenoid began to form in the center of the stroma, and RuBisCO is again concentrated in that pyrenoid region. From a comparison of photosynthetic CO2-fixation with the total carboxylase activity of RuBisCO extracted from Euglena cells in the growth phase, it is suggested that the carboxylase in the pyrenoid functions in CO2-fixation in photosynthesis.

Examination of cutaneous macroglobulinosis by immunoelectron microscopy

1996 ◽  
Vol 135 (2) ◽  
pp. 287-291 ◽  
Author(s):  
D. LIPSKER ◽  
B. CRIBIER ◽  
D. SPEHNER ◽  
N. BOEHM ◽  
E. HEID ◽  
...  
Keyword(s):  
Immunoelectron Microscopy

NMR studies of the R2 repeat and related peptide fragments of the DNA binding domain of c-Myb. New light on the structure and folding of R2.

1999 ◽  
Vol 96 (9/10) ◽  
pp. 1580-1584 ◽  
Author(s):  
I. Ségalas ◽  
S. Desjardins ◽  
H. Oulyadi ◽  
Y. Prigent ◽  
S. Tribouillard ◽  
...  
Keyword(s):  
Dna Binding ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Peptide Fragments ◽  
Nmr Studies ◽  
Related Peptide

Properties of Fibrinogen Cleaved by Jararhagin, a Metalloproteinase from the Venom of Bothrops jararaca

1994 ◽  
Vol 72 (02) ◽  
pp. 244-249 ◽  
Author(s):  
Aura S Kamiguti ◽  
Joseph R Slupsky ◽  
Mirko Zuzel ◽  
Charles R M Hay
Keyword(s):  
Platelet Aggregation ◽  
Platelet Function ◽  
Fibrin Clot ◽  
Clot Formation ◽  
Human Fibrinogen ◽  
Activated Platelets ◽  
Bothrops Jararaca ◽  
Platelet Binding ◽  
Fibrin Monomers ◽  
Fibrinogen Molecule

SummaryHaemorrhagic metalloproteinases from Bothrops jararaca and other venoms degrade vessel-wall and plasma proteins involved in platelet plug and fibrin clot formation. These enzymes also cause proteolytic digestion of fibrinogen which has been suggested to cause defective platelet function. Fibrinogen degradation by jararhagin, a metalloproteinase from B. jararaca, and the effect of jararhagin fibrinogenolysis on both platelet aggregation and fibrin clot formation were investigated. Jararhagin was found to cleave human fibrinogen in the C-terminal region of the Aα-chain giving rise to a 285-290 kDa fibrinogen molecule lacking the Aα-chain RGD 572-574 platelet-binding site. Platelet binding and aggregation of ADP-activated platelets is unaffected by this modification. This indicates that the lost site is not essential for platelet aggregation, and that the remaining platelet binding sites located in the N-terminal portion of Aα chains (RGD 95-97) and the C-terminal of γ chains (dodecapeptide 400-411) are unaffected by jararhagin-digestion of fibrinogen. Fibrin clot formation with thrombin of this remnant fibrinogen molecule was defective, with poor polymerization of fibrin monomers but normal release of FPA. The abnormal polymerization could be explained by the loss of one of the two complementary polymerization sites required for side-by-side association of fibrin protofibrils. Jararhagin-induced inhibition of platelet function, an important cause of haemorrhage in envenomed patients, is not caused by proteolysis of fibrinogen, as had been thought, and the mechanism remains to be elucidated.

Common Antigenic Sites in Human, Bovine and Porcine Fibrinogens

1981 ◽  
Vol 45 (02) ◽  
pp. 169-172 ◽  
Author(s):  
Czeslaw S Cierniewski
Keyword(s):  
Antigenic Determinants ◽  
Antigenic Sites ◽  
Specific Antisera ◽  
Antigenic Homology ◽  
Polypeptide Chains ◽  
Fibrinogen Molecule

SummarySpecific antisera to the Aα, Bβ and γ chains of porcine fibrinogen were used to characterize an antigenic homology of human, bovine, and porcine fibrinogens. Antigenic determinants shared by these fibrinogens were mostly formed by the Aα chain. However, in the case of bovine and porcine fibrinogens they were also found in the Bβ and γ polypeptide chains. The results reported here show that the Aα chain determinants exposed on the intact fibrinogen molecule are conserved to a considerably larger extent than those of the Bβ and γ chains.

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