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 Ultrastructural localization of the C-propeptide released from type II procollagen in fetal bovine growth plate cartilage.

1996 ◽  
Vol 44 (5) ◽  
pp. 433-443 ◽  
Author(s):  
E R Lee ◽  
C E Smith ◽  
R Poole
Keyword(s):  
Growth Plate ◽  
Ultrastructural Localization ◽  
Collagen Fibrils ◽  
Type Ii ◽  
Guanidinium Hydrochloride ◽  
High Affinity ◽  
Sds Page ◽  
The Matrix ◽  
Fetal Bovine ◽  
Mineralized Matrix

We used immunochemical and immunoelectron gold techniques to determine whether the C-propeptide previously identified in the matrix of endochondral cartilage (CPII) was still a part of the Type 11 procollagen molecule or had been released from it. Guanidinium hydrochloride extraction, followed by SDS-PAGE and Western blotting techniques and immunoelectron localization, revealed that predominantly only the released form (hereafter referred to as released CPII) was detected. The ultrastructural distribution of this CPII was examined with affinity-purified antibodies and with immunogold or immunoperoxidase localization techniques in the presence or absence of embedding resins. These methods yielded similar results. Although no significant amount of this CPII was retained in the matrix after guanidinium hydrochloride extraction, it was present in two recognizable sites under normal conditions, i.e., locally concentrated in a random association with collagen fibrils in the nonmineralized matrix and mainly concentrated in interfibrillar mineralizing sites in the mineralized matrix. These results suggest that the C-propeptide that has been released from Type II procollagen associates with collagen fibrils and then preferentially associates with mineralizing sites when these form in the endochondral cartilage. The significance of this preference for mineral is not known but may have something to do with its high affinity for hydroxyapatite.

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

Immunoradiometric assay with use of magnetizable particles: measurement of thyrotropin in blood spots, to screen for neonatal hypothyroidism.

1986 ◽  
Vol 32 (10) ◽  
pp. 1966-1968 ◽  
Author(s):  
K V Waite ◽  
G F Maberly ◽  
G Ma ◽  
C J Eastman
Keyword(s):  
Incubation Time ◽  
Separation Procedure ◽  
Immunoradiometric Assay ◽  
Assay Sensitivity ◽  
Neonatal Hypothyroidism ◽  
Blood Spots ◽  
Standard Curve ◽  
Coefficients Of Variation ◽  
Specialized Equipment ◽  
Short Incubation Time

Abstract We adapted a commercial immunoradiometric assay (IRMA) to measure thyrotropin in filter-paper blood spots. Two 3-mm blood spots are used for each standard and sample. These are incubated for 2 h with radiolabeled antibody and for 30 min with magnetic antibody, followed by a 10-min separation procedure. Assay sensitivity is 6 milli-int. units/L. Coefficients of variation (precision profile of the standard curve) ranged from 4.3 to 9.6%. The coefficient of correlation (r) between thyrotropin concentrations in the blood spots and in serum was 0.93. Pre-elution of the blood spots is necessary for short incubation time. Short incubation time, little need for specialized equipment, the high precision and sensitivity characteristic of IRMA, and ease of collection, transport, and storage of the blood-spot samples make this assay suitable for neonatal hypothyroid screening.

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