Formation of lipid peroxides in isolated rat liver microsomes by Singlet molecular oxygen

1977 ◽  
Vol 17 (3) ◽  
pp. 376
Keyword(s):  
Molecular Oxygen ◽  
Rat Liver ◽  
Liver Microsomes ◽  
Lipid Peroxides ◽  
Rat Liver Microsomes ◽  
Singlet Molecular Oxygen ◽  
Isolated Rat Liver ◽  
Isolated Rat

scholarly journals Characterization and biosynthesis of cytochrome b5 in rat liver microsomes

1968 ◽  
Vol 107 (6) ◽  
pp. 839-849 ◽  
Author(s):  
J. R. Sargent ◽  
B. P. Vadlamudi
Keyword(s):  
Amino Acid ◽  
Rat Liver ◽  
Spectral Properties ◽  
Proteolytic Enzymes ◽  
Cytochrome B5 ◽  
Liver Microsomes ◽  
Rat Liver Microsomes ◽  
Isolated Rat Liver ◽  
Peptide Linkage ◽  
Isolated Rat

1. Cytochrome b5 is released from rat liver microsomes by both proteolytic enzymes and by treatments that disrupt phospholipids. Cytochrome P-420 is only released to a marked extent by treatments that disrupt phospholipids. 2. Cytochrome b5 was isolated in a pure state from both the rough and smooth fractions of rat liver microsomes after treatment with trypsin, and was shown to contain two cytochrome components with identical spectral properties. 3. Amino acid analyses of the two components are presented, together with peptide ‘fingerprint’ patterns of tryptic digests of the two components. 4. Studies based on the direct isolation of cytochrome b5 after administration of a single dose of radioactive amino acid to rats demonstrate that the cytochrome is synthesized initially in the rough fraction of microsomes and only subsequently appears in the smooth fraction. 5. Isolated rat liver microsomes are capable of incorporating radioactive amino acids into cytochrome b5 under standard conditions. 6. Under these conditions the amino acid is incorporated into peptide linkage in the cytochrome.

scholarly journals Inhibition of phosphatidylcholine synthesis by vasopressin and angiotensin in rat hepatocytes

1982 ◽  
Vol 208 (2) ◽  
pp. 453-457 ◽  
Author(s):  
S Alemany ◽  
I Varela ◽  
J M Mato
Keyword(s):  
Rat Liver ◽  
Liver Microsomes ◽  
Rat Hepatocytes ◽  
Rat Liver Microsomes ◽  
Isolated Rat Hepatocytes ◽  
Fast Transient ◽  
Phosphatidylcholine Synthesis ◽  
Isolated Rat

The addition of 1 microM-vasopressin or -angiotensin to isolated rat hepatocytes induced a fast transient inhibition of the rate of incorporation of [Me-3H]choline into phosphatidylcholine. The cationophore A23187 induced a similar inhibition of phosphatidylcholine synthesis. The addition of micromolar Ca2+ to rat liver microsomes inhibited the activity of CDP-choline: 1,2-diacylglycerol cholinephosphotransferase. This inhibition is due a decrease in the Vmax. of the enzyme without affecting the Km for CDP-choline. It is concluded that Ca2+ regulates phosphatidylcholine synthesis in rat liver.

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