The green hemoproteins of bovine erythrocytes. I purification and characterization.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference25 articles.
1. A New Hæmoprotein with a Unique Iron Porphyrin Prosthetic Group isolated from Human Erythrocytes
2. Purification and properties of an erythrocyte hemoprotein with a unique prosthetic group
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4. The Molar Light Absorption of Pyridine Ferroprotoporphrin (Pyridine Haemochromogen).
5. The Reliability of Molecular Weight Determinations by Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis
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1. Evidence that NADPH-dependent methemoglobin reductase and administered riboflavin protect tissues from oxidative injury;American Journal of Hematology;1993-01
2. Evidence that the protein components of bovine erythrocyte green heme binding protein and flavin reductase are identical;Biochemical and Biophysical Research Communications;1991-07
3. Molecular characteristics of many hemoproteins: A survey of molecular weights, sedimentation coefficients, other molecular parameters and amino acid compositions;Journal of Theoretical Biology;1987-11
4. Spectroscopic properties of spinach catalase;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1987-01
5. Spectroscopic, ligand binding, and enzymatic properties of the spleen green hemeprotein. A comparison with myeloperoxidase.;Journal of Biological Chemistry;1985-09
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