scholarly journals Enantiotopic Demethylation of Fenitrothion into Partially Racemized (R)p-(+)-Desmethylfenitrothion by Mouse Liver Homogenate and Mice

1983 ◽  
Vol 8 (1) ◽  
pp. 115-120 ◽  
Author(s):  
Akio MIYAZAKI ◽  
Mitsuo KAWARADANI ◽  
Shingo MARUMO ◽  
Chojiro TOMIZAWA
Keyword(s):  
Mouse Liver ◽  
Liver Homogenate

Conversion of 3-Hydroxykynurenine to 4,8-Dihydroxyquinoline by Mouse Liver Homogenate

Science ◽  
1955 ◽  
Vol 121 (3135) ◽  
pp. 143-144 ◽  
Author(s):  
K. Makino ◽  
K. Arai
Keyword(s):  
Mouse Liver ◽  
Liver Homogenate

INTRACELLULAR DISTRIBUTION OF PHOSPHOMONOESTERASES IN RAT LIVER HOMOGENATE

1954 ◽  
Vol 32 (1) ◽  
pp. 383-394 ◽  
Author(s):  
Claude Allard ◽  
Gaston de Lamirande ◽  
Hugo Faria ◽  
Antonio Cantero
Keyword(s):  
Acid Phosphatase ◽  
Rat Liver ◽  
Mouse Liver ◽  
Soluble Fraction ◽  
Liver Homogenate ◽  
Mitochondrial Fraction ◽  
Nuclear Fraction ◽  
Absolute Requirement ◽  
Rat Liver Cells ◽  
Liver Homogenates

Acid phosphatase or phosphomonoesterase II activity of rat and mouse liver homogenates, prepared in 0.25 M sucrose, was found mainly in the cytoplasmic granules. Since the small percentage of activity of the nuclear fraction activity could be explained by the presence of mitochondria (which were actually counted in this fraction) it is concluded that rat and mouse liver nuclei do not contain acid phosphatase activity.A rather broad range of acid phosphatase activity was observed in rat and mouse livers depending on the time elapsed between the preparation of homogenate and the activity determinations. However, a preincubation of the tissues or isolated fractions at 37° C. for 60 min. was sufficient to increase the activity to an optimal value, and thus eliminate variations due to the latency of this enzyme.Alkaline phosphatase or phosphomonoesterase I activity was also found to be latent in rat liver homogenates. The phenomenon was less apparent than for acid phosphatase and seemed to depend mostly on the nature of the buffer employed in the assay system.Some evidence for the presence of two forms of alkaline phosphatase in rat liver cells is presented. One form of the enzyme was found to have an absolute requirement of magnesium for activity and was present in the soluble fraction, whereas the other which was not activated by magnesium seemed firmly linked to the nuclei and microsomes and was absent in the soluble fraction. The activity in the mitochondrial fraction was small and seemed of doubtful significance.

scholarly journals Comparative proteomic analysis of mouse liver and brain isatin-binding proteins

2018 ◽  
Vol 1 (1) ◽  
pp. e00007 ◽  
Author(s):  
O.A. Buneeva ◽  
A.T. Kopylov ◽  
V.G. Zgoda ◽  
A.E. Medvedev
Keyword(s):  
Lipid Metabolism ◽  
Proteomic Analysis ◽  
Mouse Liver ◽  
Binding Proteins ◽  
Biological Activities ◽  
Regulation Of Gene Expression ◽  
Liver Homogenate ◽  
Comparative Proteomic Analysis ◽  
Protective Proteins ◽  
The Brain

Isatin (indol-2,3-dione) is an endogenous indole, exhibiting various biological activities that are realized via its interacts with numerous target proteins (so-called isatin-binding proteins). To date, isatin-binding proteins have been characterized in the brain of mice and rats. In this study we have performed a comparative proteomic analysis of the isatin-binding proteins of the mouse liver and brain. Proteomic profiling of clarified lysates of membrane and soluble fractions of liver and brain homogenates was performed using 5-aminocaproyl-isatin as an affinity ligand. During affinity based separation of isatin-binding proteins of soluble and membrane fractions of mouse brain homogenates lysed with Triton X-100, 63 individual proteins were identified. A similar separation of mouse liver homogenate fractions during affinity chromatography resulted in identification of 80 proteins. All identified liver and brain proteins belonged to the following functional groups: (I) Carbohydrate metabolism and energy generation; (II) Lipid metabolism; (III) Metabolism of nucleotides and amino acids; (IV) Formation of the cytoskeleton, exocytosis; (V) Regulation of gene expression, cell division and differentiation; (VI) Antioxidant and protective proteins; (VII) Signal transmission and regulation of enzyme activity. The total number of isatin-binding proteins common for the brain and liver was only 12. The most common for the brain and liver of isatin-binding proteins was found in group VI (antioxidant and protective proteins), complete absence of coincidence in group II (lipid metabolism) and group IV (formation of the cytoskeleton, exocytosis). The observed differences in the profile of isatin-binding proteins appear to play an important role in the specific effects of isatin in certain organs.

INTRACELLULAR DISTRIBUTION OF PHOSPHOMONOESTERASES IN RAT LIVER HOMOGENATE

1954 ◽  
Vol 32 (4) ◽  
pp. 383-394 ◽  
Author(s):  
Claude Allard ◽  
Gaston de Lamirande ◽  
Hugo Faria ◽  
Antonio Cantero
Keyword(s):  
Acid Phosphatase ◽  
Rat Liver ◽  
Mouse Liver ◽  
Soluble Fraction ◽  
Liver Homogenate ◽  
Mitochondrial Fraction ◽  
Nuclear Fraction ◽  
Absolute Requirement ◽  
Rat Liver Cells ◽  
Liver Homogenates

Acid phosphatase or phosphomonoesterase II activity of rat and mouse liver homogenates, prepared in 0.25 M sucrose, was found mainly in the cytoplasmic granules. Since the small percentage of activity of the nuclear fraction activity could be explained by the presence of mitochondria (which were actually counted in this fraction) it is concluded that rat and mouse liver nuclei do not contain acid phosphatase activity.A rather broad range of acid phosphatase activity was observed in rat and mouse livers depending on the time elapsed between the preparation of homogenate and the activity determinations. However, a preincubation of the tissues or isolated fractions at 37° C. for 60 min. was sufficient to increase the activity to an optimal value, and thus eliminate variations due to the latency of this enzyme.Alkaline phosphatase or phosphomonoesterase I activity was also found to be latent in rat liver homogenates. The phenomenon was less apparent than for acid phosphatase and seemed to depend mostly on the nature of the buffer employed in the assay system.Some evidence for the presence of two forms of alkaline phosphatase in rat liver cells is presented. One form of the enzyme was found to have an absolute requirement of magnesium for activity and was present in the soluble fraction, whereas the other which was not activated by magnesium seemed firmly linked to the nuclei and microsomes and was absent in the soluble fraction. The activity in the mitochondrial fraction was small and seemed of doubtful significance.

Sign in / Sign up

Export Citation Format

Share Document