scholarly journals Some Marker Enzymes and Histological Alteration on the Administration of Tramadol Hydrochloride on Rat Liver

2018 ◽  
Vol 07 (01) ◽  
pp. 9-20
Author(s):  
George Gborienemi Simeon ◽  
Silas Tonye Abbey
Keyword(s):  
Rat Liver ◽  
Marker Enzymes ◽  
Tramadol Hydrochloride ◽  
Histological Alteration

Analytical Subcellular Fractionation Studies on Rat Liver and on Isolated Jejunal Enterocytes with Special Reference to the Separation of Lysosomes, Peroxisomes and Mitochondria

1976 ◽  
Vol 50 (5) ◽  
pp. 355-366 ◽  
Author(s):  
T. J. Peters ◽  
H. Shio
Keyword(s):  
Rat Liver ◽  
Sucrose Density Gradient ◽  
Subcellular Fractionation ◽  
Low Molecular Weight ◽  
Rat Jejunum ◽  
Marker Enzymes ◽  
Good Separation ◽  
Subcellular Organelles ◽  
Rat Liver Cells ◽  
Isopycnic Centrifugation

1. Enterocytes were isolated from rat jejunum and characterized morphologically. 2. Attempts to separate the enterocyte subcellular organelles, characterized by their marker enzymes, with isopycnic centrifugation were unsuccessful but good separation of peroxisomes, lysosomes and mitochondria was achieved by sedimentation through a shallow sucrose density gradient with a superimposed inverse gradient of low-molecular-weight dextran. 3. The properties and enzyme activities of the principal subcellular organelles in rat liver cells and enterocytes were compared.

scholarly journals Isolation of autophagic vacuoles from rat liver: morphological and biochemical characterization.

1982 ◽  
Vol 93 (1) ◽  
pp. 144-154 ◽  
Author(s):  
L Marzella ◽  
J Ahlberg ◽  
H Glaumann
Keyword(s):  
Proteolytic Activity ◽  
Rat Liver ◽  
Biochemical Characterization ◽  
Secretory Granules ◽  
Density Lipoprotein ◽  
Marker Enzymes ◽  
Cell Organelles ◽  
Protein Ratio ◽  
Autophagic Vacuoles

The induction of autophagy caused by vinblastine (VBL) has been found to be concomitant with a stimulation of proteolysis in a mitochondrial-lysosomal (ML) fraction from the rat liver (Marzella and Glaumann, 1980, Lab. Invest., 42: 8-17. Marzella and Glaumann, 1980, Lab. Invest., 42:18-27). In this fraction the enhanced proteolysis is associated with a threefold increase in the relative fractional volume of autophagic vacuoles (AVs). In an attempt to isolate the AVs, we subfractionated the ML suspension at different intervals after the induction of autophagy by VBL by centrifugation on a discontinuous Metrizamide gradient ranging from 50% to 15%. The material banding at the 24 to 20% and the 20 to 15% interphases was collected. Morphological analysis reveals that 3 h after induction of autophagy these fractions consist predominantly (approximately 90%) of intact autophagic vacuoles. These autophagic vacuoles contain cytosol, mitochondria, portions of endoplasmic reticulum, and occasional very low density lipoprotein, particles either free or in Golgi apparatus derivatives, in particular secretory granules. The sequestered materials show ultrastructural signs of ongoing degradation. In addition to containing typical autophagic vacuoles, the isolated fractions consist of lysosomes lacking morphologically recognizable cellular components. Contamination from nonlysosomal material is only a few percent as judged from morphometric analysis. Typical lysosomal "marker" enzymes are enriched 15-fold, whereas the proteolytic activity is enriched 10- to 20-fold in the isolated AV fraction as compared to the homogenate. Initially, the yield of nonlysosomal mitochondrial and microsomal enzyme activities increases in parallel with the induction of autophagy but, later on, decreases with advanced degradation of the sequestered cell organelles. Therefore, in the case of AVs the presence of nonlysosomal marker enzymes cannot be used for calculation of fraction purity, since newly sequestered organelles are enzymatically active. Isolated autophagic vacuoles show proteolytic activity when incubated in vitro. The comparatively high phospholipid/protein ratio (0.5) of the AV fraction suggests that phospholipids are degraded more slow than proteins. Is it concluded that AVs can be isolated into a pure fraction and are the subcellular site of enhanced protein degradation in the rat liver after induction of autophagy.

Taurocholate transport by basolateral plasma membrane vesicles isolated from developing rat liver

1985 ◽  
Vol 248 (6) ◽  
pp. G648-G654
Author(s):  
F. J. Suchy ◽  
S. M. Courchene ◽  
B. L. Blitzer
Keyword(s):  
Plasma Membrane ◽  
Rat Liver ◽  
Basolateral Membrane ◽  
Membrane Vesicles ◽  
Marker Enzyme ◽  
Marker Enzymes ◽  
Plasma Membrane Vesicles ◽  
Adult Rat ◽  
Basolateral Plasma Membrane ◽  
Taurocholate Transport

Taurocholate transport was characterized in basolateral plasma membrane vesicles prepared from the livers of 14-day-old Sprague-Dawley rats using a self-generating Percoll gradient method. Liver plasma membrane protein yield, intravesicular volume, and enrichments of various marker enzymes were similar to those obtained for vesicles from adult rat liver. The basolateral marker enzyme Na+-K+-ATPase was enriched 26-fold in the suckling rat basolateral membrane fraction while the bile canalicular marker enzymes alkaline phosphatase and Mg2+-ATPase were enriched only 3- and 5-fold, respectively. The activities of marker enzymes for endoplasmic reticulum, mitochondria, or lysosomes were not enriched compared with homogenate. In the presence of an inwardly directed 100 mM Na+ gradient, vesicle accumulation of taurocholate transiently reached a concentration 1.5- to 2-fold higher than that at equilibrium ("overshoot") in suckling and adult membrane vesicles, but the initial rate of taurocholate entry and peak intravesicular accumulation were markedly decreased in suckling compared with adult membrane vesicles. In the presence of an inwardly directed 100 mM K+ gradient, the rate of uptake was slower, and no overshoot occurred in either suckling or adult rat vesicles. The decreased rate of Na+-coupled taurocholate uptake by membrane vesicles from suckling rat liver could not be explained on the basis of more rapid dissipation of the transmembrane Na+ gradient. Kinetic studies demonstrated saturable, Na+-dependent taurocholate uptake for both suckling and adult vesicles. However, the Vmax for taurocholate uptake in suckling rat vesicles was less than half of the adult rate (2.46 +/- 0.13 vs. 5.25 +/- 0.22 nmol X mg prot-1 X min-1, respectively, P less than 0.001).(ABSTRACT TRUNCATED AT 250 WORDS)

Gel filtration of marker enzymes of plasma membrane and endoplasmic reticulum from rat liver

1969 ◽  
Vol 193 (2) ◽  
pp. 468-471 ◽  
Author(s):  
Kenji Nakai ◽  
Shigehide Takemitsu ◽  
Toshisuke Kawasaki ◽  
Ikuo Yamashina
Keyword(s):  
Endoplasmic Reticulum ◽  
Plasma Membrane ◽  
Rat Liver ◽  
Gel Filtration ◽  
Marker Enzymes

Evidence for the Biosynthetic Difference between Isolated Mitochondria and Microsomes from Guinea-Pig and Rat Liver Regarding Lysophospharidic Acid, Phosphatidic Acid, CDP-Diglyceride, Phosphatidylglycerol, and Cardiolipin

1974 ◽  
Vol 52 (10) ◽  
pp. 936-939 ◽  
Author(s):  
J. B. Davidson ◽  
N. Z. Stanacev
Keyword(s):  
Guinea Pig ◽  
Phosphatidic Acid ◽  
Rat Liver ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Marker Enzymes ◽  
Synthetic Enzymes ◽  
Isolated Mitochondria ◽  
Significant Difference ◽  
Nadph Cytochrome C Reductase

The enzymatic activities of marker enzymes (NADPH – cytochrome c reductase and glucose-6-phosphatase) and synthetic enzymes (acyl-CoA:sn-glycero-3-phosphate acyltransferase, CTP:sn-3-phosphatidic acid cytidyltransferase, and CDP-diglyceride:sn-glycero-3-phosphate phosphatidyltransferase) were measured in both isolated mitochondria and microsomes from liver of guinea pig and rat. Results thus obtained show a significant difference in activities of these enzymes between subcellular particles within species and between two examined species. The activity of acyl-CoA:glycero-3-phosphate acyltransferase in guinea-pig mitochondria parallels the activity of microsomal marker enzymes in this fraction, while in rat liver mitochondria the activity is relatively higher and cannot be accounted for by the microsomal content as determined by marker enzymes. Implications of these results regarding mitochondrial autonomy in the biosynthesis of polyglycero-phosphatides and their precursors are discussed.

Effect of Strobilanthes crispus on the Histology and Tumour Marker Enzymes in Rat Liver During Hepatocarcinogenesis

2005 ◽  
Vol 5 (2) ◽  
pp. 130-135 ◽  
Author(s):  
Suherman Jaksa ◽  
Asmah Rahmat . ◽  
Fauziah Othman . ◽  
Patimah Ismail . ◽  
Siti Muskinah Hj. Ma .
Keyword(s):  
Rat Liver ◽  
Tumour Marker ◽  
Marker Enzymes ◽  
Strobilanthes Crispus

scholarly journals Studies on the glutathione S-transferase activity associated with rat liver mitochondria

1984 ◽  
Vol 222 (2) ◽  
pp. 553-556 ◽  
Author(s):  
C M Ryle ◽  
T J Mantle
Keyword(s):  
Lactate Dehydrogenase ◽  
Rat Liver ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Transferase Activity ◽  
Marker Enzymes ◽  
Glutathione S Transferase ◽  
Mitochondrial Marker ◽  
Liver Glutathione

The major proportion of rat liver glutathione S-transferase is cytosolic. Carefully washed mitochondria contain 0.25-0.47% of the cytosolic activity. Subfractionation of washed mitochondria using digitonin treatment revealed that glutathione S-transferase release did not parallel that of any of the mitochondrial marker enzymes. Glutathione S-transferase release paralleled that of lactate dehydrogenase, suggesting that these ‘mitochondrial’ activities are due to loosely bound cytoplasmic forms.

scholarly journals Subcellular localization of ornithine decarboxylase in liver of control and growth-hormone-treated rats

1976 ◽  
Vol 157 (1) ◽  
pp. 33-39 ◽  
Author(s):  
B J Murphy ◽  
M E Brosnan
Keyword(s):  
Growth Hormone ◽  
Ornithine Decarboxylase ◽  
Rat Liver ◽  
Subcellular Fractionation ◽  
Decarboxylase Activity ◽  
Differential Centrifugation ◽  
Marker Enzymes ◽  
Aminotransferase Activity ◽  
Apparent Affinity ◽  
Hormone Administration

1. Ornithine-2-oxo acid aminotransferase activity was inhibited by amino-oxyacetate (10(-5) M). This permitted the measurement of ornithine decarboxylase in the presence of mitochondria by using the 14CO2-trapping technique. 2. Subcellular fractionation of rat liver by differential centrifugation, followed by the assay of ornithine decarboxylase in the presence of amino oxyacetate and of marker enzymes for each fraction, demonstrated that ornithine decarboxylase was located in the cytosol. 3. The greatly increased ornithine decarboxylase activity observed after growth-hormone administration was also found to be localized in the cytosol. 4. The Km of ornithine decarboxylase from rat liver for ornithine was 28 muM. Administration of growth hormone 4 h before death did not affect the apparent affinity of ornithine decarboxylase for ornithine.

Effect of the antilipolytic compound acipimox on peroxisome marker enzymes, lipid pattern and biotransformation related functions in rat liver

1985 ◽  
Vol 17 (10) ◽  
pp. 927-936 ◽  
Author(s):  
Gaetano Orsini ◽  
Pier Paolo Lovisolo ◽  
Augusto Chiari ◽  
Umberto Branzoli
Keyword(s):  
Rat Liver ◽  
Marker Enzymes ◽  
Lipid Pattern
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