scholarly journals LIGHT MICROSCOPIC STUDY OF THE PEROXIDATIC ACTIVITY OF CATALASE IN FORMALDEHYDE-FIXED RAT LIVER

1969 ◽  
Vol 17 (9) ◽  
pp. 585-590 ◽  
Author(s):  
KEI-ICHI HIRAI
Keyword(s):  
Hydrogen Peroxide ◽  
Microscopic Study ◽  
Rat Liver ◽  
Incubation Medium ◽  
Histochemical Staining ◽  
Hydrogen Donor ◽  
Peroxidatic Activity ◽  
Light Microscopic Study ◽  
Parenchymal Cells

The peroxidatic activity of rat liver catalase was demonstrated by histochemical staining with 3,3'-diaminobenzidine as hydrogen donor. The activity was so weak that its location was hard to identify in formaldehyde-fixed cells, although high catalatic activity was present, as evidenced by the production of bubbles upon the addition of hydrogen peroxide to the incubation medium. Pretreatment of fixed sections for 60 min at 37°C with formamide, urea or trypsin enhanced the peroxidatic activity significantly. The reaction granules scattered throughout the cytoplasm of the parenchymal cells probably correspond to the peroxisomes.

Different localizations of met-enkephalin-like immunoreactivity in rat forebrain and spinal cord using hydrogen peroxide and Triton X-100. Light microscopic study

1983 ◽  
Vol 11 (5) ◽  
pp. 555-571 ◽  
Author(s):  
Michel Arluison ◽  
Marie Conrath-Verrier ◽  
Michel Tauc ◽  
Phillippe Mailly ◽  
Irudayanadin Séraphin De La Manche ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Spinal Cord ◽  
Microscopic Study ◽  
Rat Forebrain ◽  
Light Microscopic Study ◽  
Triton X

scholarly journals Kinetics and mechanisms of catalase in peroxisomes of the mitochondrial fraction

1971 ◽  
Vol 122 (2) ◽  
pp. 225-233 ◽  
Author(s):  
B. Chance ◽  
N. Oshino
Keyword(s):  
Hydrogen Peroxide ◽  
Rat Liver ◽  
Fold Increase ◽  
Mitochondrial Fraction ◽  
Hydrogen Donor ◽  
Urate Oxidase ◽  
Mitochondrial Fractions ◽  
Hydrogen Peroxide Generation ◽  
State 1

1. The primary intermediate of catalase and hydrogen peroxide was identified and investigated in peroxisome-rich mitochondrial fractions of rat liver. On the basis of kinetic constants determined in vitro, it is possible to calculate with reasonable precision the molecular statistics of catalase action in the peroxisomes. 2. The endogenous hydrogen peroxide generation is adequate to sustain a concentration of the catalase intermediate (pm/e) of 60–70% of the hydrogen peroxide saturation value. Total amount of catalase corresponds to 0.12–0.15nmol of haem iron/mg of protein. In State 1 the rate of hydrogen peroxide generation corresponds to 0.9nmol/min per mg of protein or 5′ of the mitochondrial respiratory rate in State 4. 3. Partial saturation of the catalase intermediate with hydrogen peroxide (pm/e) in the mitochondrial fraction suggests its significant peroxidatic activity towards its endogenous hydrogen donor. A variation of this value (pm/e) from 0.3 in State 4 to 0 under anaerobic conditions is observed. 4. For a particular preparation the hydrogen peroxide generation rate in the substrate-supplemented State 4 corresponds to 0.17s-1 (eqn. 6), the hydrogen peroxide concentration to 2.5nm and the hydrogen-donor concentration (in terms of ethanol) to 0.12mm. The reaction is 70% peroxidatic and 30′ catalatic. 5. A co-ordinated production of both oxidizing and reducing substrates for catalase in the mitochondrial fraction is suggested by a 2.2-fold increase of hydrogen peroxide generation and a threefold increase in hydrogen-donor generation in the State 1 to State 4 transition. 6. Additional hydrogen peroxide generation provided by the urate oxidase system of peroxisomes (8–12nmol of uric acid oxidized/min per mg of protein) permits saturation of the catalase with hydrogen peroxide to haem occupancy of 40′ compared with values of 36′ for a purified rat liver catalase ofk1=1.7×107m-1·s-1 and k′4=2.6×107m-1· s-1(Chance, Greenstein & Roughton, 1952). 7. The turnover of the catalase ethyl hydrogen peroxide intermediate (k′3) in the peroxisomes is initially very rapid since endogenous hydrogen peroxide acts as a hydrogen donor. k′3 decreases fivefold in the uncoupled state of the mitochondria.

scholarly journals Induction of amino acid transport in primary cultures of adult rat liver parenchymal cells by insulin.

1976 ◽  
Vol 251 (10) ◽  
pp. 3014-3020 ◽  
Author(s):  
R F Kletzien ◽  
M W Pariza ◽  
J E Becker ◽  
V R Potter ◽  
F R Butcher
Keyword(s):  
Amino Acid ◽  
Rat Liver ◽  
Amino Acid Transport ◽  
Primary Cultures ◽  
Acid Transport ◽  
Liver Parenchymal ◽  
Adult Rat ◽  
Parenchymal Cells
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