Purification and characterization of cytosolic liver protein facilitating heme transport into apocytochrome b5 from mitochondria. Evidence for identifying the heme transfer protein as belonging to a group of glutathione S-transferases.-Reference-Cited by-同舟云学术

Purification and characterization of cytosolic liver protein facilitating heme transport into apocytochrome b5 from mitochondria. Evidence for identifying the heme transfer protein as belonging to a group of glutathione S-transferases.

Published:1985-08 Issue:16 Volume:260 Page:9191-9196
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Senjo M,Ishibashi T,Imai Y

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference36 articles.

1. Enzyme Topology of Intracellular Membranes

2. The structural organization of haem synthesis in rat liver mitochondria

3. Phenobarbital induction of NADPH-cytochrome c (P-450) oxidoreductase messenger ribonucleic acid

4. Cell-free translation of apocytochrome b5 messenger RNA and analysis of the peptide product

5. SOLUBLE HEPATIC -AMINOLEVULINIC ACID SYNTHETASE: END-PRODUCT INHIBITION OF THE PARTIALLY PURIFIED ENZYME

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