Structural analysis of NADPH-cytochrome P-450 reductase from porcine hepatic microsomes. Sequences of proteolytic fragments, cysteine-containing peptides, and a NADPH-protected cysteine peptide.-Reference-Cited by-同舟云学术

Structural analysis of NADPH-cytochrome P-450 reductase from porcine hepatic microsomes. Sequences of proteolytic fragments, cysteine-containing peptides, and a NADPH-protected cysteine peptide.

Published:1984-11 Issue:22 Volume:259 Page:13703-13711
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Haniu M,Iyanagi T,Legesse K,Shively J E

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference27 articles.

1. Structural features of liver microsomal NADPH-cytochrome P-450 reductase. Hydrophobic domain, hydrophilic domain, and connecting region.

2. High-sensitivity amino acid analysis: Methodology for the determination of amino acid compositions with less than 100 picomoles of peptides

3. Empirical Predictions of Protein Conformation

4. Two-column system for determination of glucosamine, galactosamine, and amino acids on a Beckman 121MB amino acid analyzer: Separation of the anomers of glucosamine and galactosamine

5. Cytochrome b5 reduction by NADPH-cytochrome P-450 reductase.

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