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

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).

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.

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

1982 ◽  
Vol 93 (1) ◽  
pp. 96-100 ◽  
Author(s):  
V. N. Baranov ◽  
N. V. �ngel'gardt ◽  
M. N. Lazareva ◽  
A. I. Gusev
Keyword(s):  
Mouse Liver ◽  
Ultrastructural Localization

Ultrastructural Localization of Acid Mucosubstance in Skeletal Muscle

1967 ◽  
Vol 25 ◽  
pp. 52-53 ◽  
Author(s):  
William J. Dougherty ◽  
Samuel S. Spicer
Keyword(s):  
Striated Muscle ◽  
Divalent Cations ◽  
Ultrastructural Localization ◽  
Major Elements ◽  
Frozen Sections ◽  
Thorium Dioxide ◽  
Iron Solution ◽  
Coupling System ◽  
Psoas Muscles ◽  
Formalin Fixed

In recent years, considerable attention has focused on the morphological nature of the excitation-contraction coupling system of striated muscle. Since the study of Porter and Palade, it has become evident that the sarcoplastic reticulum (SR) and transverse tubules constitute the major elements of this system. The problem still exists, however, of determining the mechamisms by which the signal to interdigitate is presented to the thick and thin myofilaments. This problem appears to center on the movement of Ca++ions between myofilaments and SR. Recently, Philpott and Goldstein reported acid mucosubstance associated with the SR of fish branchial muscle using the colloidal thorium dioxide technique, and suggested that this material may serve to bind or release divalent cations such as Ca++. In the present study, Hale's iron solution adapted to electron microscopy was applied to formalin-fixed myofibrils isolated from glycerol-extracted rabbit psoas muscles and to frozen sections of formalin-fixed rat psoas muscles.

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