A comparison of ultrastructural localization of carnitine acetyltransferase activity in mouse liver mitochondria with that in cardiac muscle

1971 ◽  
Vol 27 (2) ◽  
pp. 184-187 ◽  
Author(s):  
T. Makita ◽  
E. B. Sandborn
Keyword(s):  
Cardiac Muscle ◽  
Mouse Liver ◽  
Ultrastructural Localization ◽  
Liver Mitochondria ◽  
Carnitine Acetyltransferase ◽  
Acetyltransferase Activity

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 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 Effects of extramitochondrial ADP on permeability transition of mouse liver mitochondria

2005 ◽  
Vol 1706 (1-2) ◽  
pp. 98-104 ◽  
Author(s):  
Zemfira Z. Gizatullina ◽  
Ying Chen ◽  
Stephan Zierz ◽  
Frank Norbert Gellerich
Keyword(s):  
Mouse Liver ◽  
Permeability Transition ◽  
Liver Mitochondria

scholarly journals Physiological levels of formate activate mitochondrial superoxide/hydrogen peroxide release from mouse liver mitochondria

FEBS Letters ◽  
2017 ◽  
Vol 591 (16) ◽  
pp. 2426-2438 ◽  
Author(s):  
Adrian Young ◽  
Danielle Gardiner ◽  
Margaret E. Brosnan ◽  
John T. Brosnan ◽  
Ryan J. Mailloux
Keyword(s):  
Hydrogen Peroxide ◽  
Mouse Liver ◽  
Liver Mitochondria ◽  
Mitochondrial Superoxide ◽  
Hydrogen Peroxide Release

Influence of some insecticides on the ATPase of mouse liver mitochondria

1973 ◽  
Vol 10 (6) ◽  
pp. 365-367 ◽  
Author(s):  
Nancy B. Payne ◽  
Gene R. Herzberg ◽  
John L. Howland
Keyword(s):  
Mouse Liver ◽  
Liver Mitochondria
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