Ultrastructural localization of catalase on ultracryotomic sections of mouse liver by ferritin-conjugated antibody technique

1974 ◽  
Vol 40 (2) ◽  
pp. 165-174 ◽  
Author(s):  
Sadaki Yokota ◽  
Tetsuji Nagata
Keyword(s):  
Mouse Liver ◽  
Ultrastructural Localization ◽  
Antibody Technique

Ultrastructural localization of specific nucleoprotein fractions

1978 ◽  
Vol 36 (2) ◽  
pp. 204-205
Author(s):  
G. L. Brown
Keyword(s):  
Gel Electrophoresis ◽  
Mouse Liver ◽  
Polyacrylamide Gel Electrophoresis ◽  
Ultrastructural Localization ◽  
Polyacrylamide Gel ◽  
Acid Extraction ◽  
Acid Solutions ◽  
Low Salt ◽  
Liver Nuclei ◽  
Phosphate Groups

Bismuth (Bi) stains nucleoproteins (NPs) by interacting with available amino and primary phosphate groups. These two staining mechanisms are distinguishable by glutaraldehyde crosslinking (Fig. 1,2).Isolated mouse liver nuclei, extracted with salt and acid solutions, fixed in either formaldehyde (form.) or gl utaraldehyde (glut.) and stained with Bi, were viewed to determine the effect of the extractions on Bi stainina. Solubilized NPs were analyzed by SDS-polyacrylamide gel electrophoresis.Extraction with 0.14 M salt does not change the Bi staining characteristics (Fig. 3). 0.34 M salt reduces nucleolar (Nu) staining but has no effect on interchromatinic (IC) staining (Fig. 4). Proteins responsible for Nu and glut.- insensitive IC staining are removed when nuclei are extracted with 0.6 M salt (Fig. 5, 6). Low salt and acid extraction prevents Bi-Nu staining but has no effect on IC staining (Fig. 7). When nuclei are extracted with 0.6 M salt followed by low salt and acid, all Bi-staining components are removed (Fig. 8).

Fasciola hepatica: development of monoclonal antibodies against somatic antigens and their characterization by ultrastructural localization of antibody binding

1988 ◽  
Vol 62 (1) ◽  
pp. 15-28 ◽  
Author(s):  
R. E. B. Hanna ◽  
A. G. Trudgett ◽  
A. Anderson
Keyword(s):  
Monoclonal Antibodies ◽  
Fasciola Hepatica ◽  
Fluorescent Antibody ◽  
Parenchymal Cell ◽  
Ultrastructural Localization ◽  
Immunogold Labelling ◽  
Antigenic Determinants ◽  
Fluorescent Antibody Technique ◽  
Adult Fluke ◽  
Antibody Technique

ABSTRACTA series of monoclonal antibodies was prepared against tegumental and internal antigens ofFasciola hepaticaby immunizing mice with whole adult-fluke homogenates prior to harvesting the splenic lymphocytes for fusion. Preliminary screening by the Indirect Fluorescent Antibody technique indicated the occurrence of discrete groups of monoclonals differing from one another in tissue-specificity but within which IFA labelling patterns were fairly consistent. Representative hybridomas for 5 of these groups were stabilized and used to produce ascites fluid in mice. By application of an immunogold labelling technique it was possible to map the distribution of antigens for which each monoclonal antibody had affinity throughout the tissues of 4-week and 12-week flukes. Several monoclonals specifically labelled antigenic determinants on the important tegumental antigen T1. However the distribution of gold colloid labelling suggested that epitopes other than that normally exposed to the infected host were recognized; and several monoclonals specifically attached to T1 antigen in the tegument of juvenile worms only. The glycocalyx of the gut and excretory system of flukes shared T1 antigenicity with the tegument. Monoclonal antibodies were produced against an internal immunogen associated with ribosomes and heterochromatin in active protein-producing cells, and against interstitial material of adult flukes. Monoclonals against antigens in parenchymal cell cytoplasm and in mature vitelline cells were recognized but the corresponding hybridomas were not stabilized.

Ultrastructural localization of ?-fetoprotein synthesis in the regenerating mouse liver

1981 ◽  
Vol 92 (6) ◽  
pp. 1720-1724 ◽  
Author(s):  
V. B. Baranov ◽  
N. V. �ngel'gardt ◽  
M. N. Lazareva ◽  
A. I. Gusev
Keyword(s):  
Mouse Liver ◽  
Ultrastructural Localization

scholarly journals ULTRASTRUCTURAL LOCALIZATION OF A SOLUBLE COLLAGEN ANTIGEN

1971 ◽  
Vol 19 (11) ◽  
pp. 663-669 ◽  
Author(s):  
LIVIA LUSTIG
Keyword(s):  
Chick Embryo ◽  
Light And Electron Microscopy ◽  
Ultrastructural Localization ◽  
Ultrastructural Level ◽  
Collagen Fibrils ◽  
Rabbit Serum ◽  
Normal Rabbit Serum ◽  
Neutral Salt ◽  
Antibody Technique ◽  
Soluble Collagen

Soluble collagen antigen was localized at the ultrastructural level using an enzyme-labeled antibody technique. Specific antiserum against neutral salt-soluble collagen was conjugated with horseradish peroxidase. Tissue culture of fibroblasts, sections of chick embryo connective tissue and skin and tendon of newborn and adult chickens were incubated with the conjugated antiserum and processed for light and electron microscopy. Light microscopic observations showed a localization of the collagen antigen in the cytoplasm of fibroblasts and in the extracellular collagen fibers. Ultrastructurally, the antigen was found on the ribosomes, on the membranes of the rough endoplasmic reticulum, in the intracisternal material of fibroblasts and extracellularly in the collagen fibrils. The collagen fibrils of chick embryo cartilage were intensely stained while the matrix itself remained unstained. Controls performed with absorbed antiserum, conjugated normal rabbit serum or different antigens failed to react with the tissues.

scholarly journals ULTRASTRUCTURAL LOCALIZATION OF SUCCINATE DEHYDROGENASE IN MOUSE LIVER MITOCHONDRIA; A CYTOCHEMICAL STUDY

1971 ◽  
Vol 19 (2) ◽  
pp. 124-130 ◽  
Author(s):  
MOSHE KALINA ◽  
BARRY WEAVERS ◽  
A. G. E. PEARSE
Keyword(s):  
Succinate Dehydrogenase ◽  
Incubation Time ◽  
Mouse Liver ◽  
Ultrastructural Localization ◽  
Liver Mitochondria ◽  
Cytochemical Study ◽  
Prolonged Incubation ◽  
The Matrix ◽  
Transfer Chain ◽  
Short Incubation Time

Ultrastructural localization of succinate dehydrogenase, employed as a marker of the electron transfer chain, was studied in mouse liver mitochondria either in orthodox or condensed conformation. Activity of succinate dehydrogenase in the orthodox form mitochondria was localized primarily on the cristal membrane facing the matrix. A prolonged incubation time resulted in reaction product filling the intracristal space, whereas a short incubation time resulted also in a product which appeared mainly at opposite points on both sides of the crista. No such arrangement of the reaction product was noted in mitochondria in the condensed conformation. These findings, supported by studies of serial sections, suggest that the reaction product in orthodox form mitochondria appears in bands or coils surrounding the whole cristal membrane.

Ultrastructural localization of soluble and insoluble 3H-methyl prednisolone as revealed by electron microscopic dry-mounting radioautography

1978 ◽  
Vol 36 (2) ◽  
pp. 40-41
Author(s):  
T. Nagata ◽  
K. Yoshida ◽  
S. Ohno ◽  
F. Murata
Keyword(s):  
Mouse Liver ◽  
Sodium Succinate ◽  
Ultrastructural Localization ◽  
Microscopic Level ◽  
Electron Microscopic Level ◽  
Electron Microscopic ◽  
Methyl Prednisolone ◽  
Freeze Dried ◽  
Emulsion Films

IntroductionSince the recent improvements in both techniques and development in equipments at our laboratory or others, the dry-mounting procedures for radioautography facilitated the wide application of them for the study of soluble compounds such as nucleic acid precursors, amino acids, carbohydrates, lipids and steroids at both the light and electron microscopic levels. The purpose of this paper is to demonstrate ultrastructural localization of both soluble and insoluble 3H-labeled methyl prednisolone, a synthetic corticosteroid, by means of dry-mounting procedure at the electron microscopic level.Materials and MethodsMouse liver slices obtained from a male mouse and cultured HeLa cells were pulse- labeled in vitro in Eagle's MEM containing 6α-methyl prednisolone-1,2-T sodium succinate (100μCi/ml) for 1 hour.Some specimens were quickly frozen in isopentane cooled to -160°C with liquid nitrogen and freeze-dried,fixed in osmium vapour, embedded in Epon, dry-sectioned and dry-mounted according to the procedure described previously, by means of wire loops using Sakura NR-H2 emulsion containing dioctyl sodium sulfosuc- cinate in order to prevent the emulsion films from bursting while they are air dried.

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