Modulation of the reductive metabolism of halothane by microsomal cytochrome b5 in rat liver

1987 ◽  
Vol 926 (3) ◽  
pp. 231-238 ◽  
Author(s):  
Shinji Tamura ◽  
Sumio Kawata ◽  
Toshihiro Sugiyama ◽  
Seiichiro Tarui
Keyword(s):  
Rat Liver ◽  
Cytochrome B5 ◽  
Microsomal Cytochrome ◽  
Microsomal Cytochrome B5 ◽  
Reductive Metabolism

Monoclonal antibodies to rat liver microsomal cytochrome b5

1992 ◽  
Vol 43 (10) ◽  
pp. 2201-2208 ◽  
Author(s):  
Sang S. Park ◽  
Waydell Walker ◽  
Toshifumi Aoyama ◽  
David P. Lapenson ◽  
David J. Waxman ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Rat Liver ◽  
Cytochrome B5 ◽  
Microsomal Cytochrome ◽  
Microsomal Cytochrome B5

scholarly journals Studies of cytochrome synthesis in rat liver

1973 ◽  
Vol 134 (2) ◽  
pp. 377-385 ◽  
Author(s):  
Robert Druyan ◽  
Smilja Jakovcic ◽  
Murray Rabinowitz
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Rat Liver ◽  
Cytochrome B5 ◽  
Liver Protein ◽  
Protein Synthesis Inhibitors ◽  
Microsomal Cytochrome ◽  
Microsomal Cytochrome B5 ◽  
Parallel Fashion

The incorporation of radioactive amino acids and of δ-amino[2,3-3H2]laevulinate into rat liver cytochromes b5 and c and cytochrome oxidase has been examined with and without protein-synthesis inhibitors. Cycloheximide promptly inhibits labelling of both haem and protein for cytochrome c in parallel fashion. Although incorporation of 14C-labelled amino acid into microsomal cytochrome b5 is also rapidly inhibited, cycloheximide incompletely inhibits haem labelling of cytochrome b5 and cytochrome a+a3, and inhibition occurs only after repeated antibiotic injections. The possibility of apo-protein pools, or of haem exchange, with a rapidly renewed ‘free’ haem pool, is considered. Consistent with this model is the observation of non-enzymic haem exchange in vitro between cytochrome b5 and methaemoglobin. Chloramphenicol, injected intravenously over 5h, results in a 20–40% decrease in incorporation of δ-amino[2,3-3H2]laevulinate into haem a+a3 and haem of cytochromes b5 and c. With the dosage schedule of chloramphenicol studied, amino acid labelling of total liver protein and of cytochrome c was not inhibited. Similarly, ferrochelatase activity was not decreased.

More similarity between bakers' yeast L-(+)-lactate dehydrogenase and liver microsomal cytochrome b5

Nature ◽  
1975 ◽  
Vol 255 (5507) ◽  
pp. 422-423 ◽  
Author(s):  
BERNARD GUIARD ◽  
FLORENCE LEDERER ◽  
C. JACQ
Keyword(s):  
Lactate Dehydrogenase ◽  
Cytochrome B5 ◽  
Microsomal Cytochrome ◽  
Microsomal Cytochrome B5
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