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Interaction of hemopexin, albumin and liver fatty acid-binding protein with protoporphyrin. 1989

E Knobler, and M B Poh-Fitzpatrick, and D Kravetz, and W R Vincent, and U Muller-Eberhard, and S H Vincent
Department of Dermatology, Columbia University College of Physicians and Surgeons, New York, New York 10032.

Equilibrium constants for the binding of protoporphyrin to serum albumin and hemopexin and liver cytosolic fatty acid-binding protein of the rat were determined fluorometrically. The experimental equilibrium constant [10(6) M-1 (mean +/- S.D.)] values were 8.4 +/- 1.3, 10.0 +/- 2.4 and 34.0 +/- 3.0 for albumin, hemopexin and liver fatty acid-binding protein, respectively. Statistical analysis showed the equilibrium constant of binding of protoporphyrin to liver fatty acid-binding protein to be significantly (p less than 0.01) higher than that to albumin and hemopexin. The data suggest that in patients with erythropoietic protoporphyria an equilibrium gradient may exist which favors the uptake by hepatocytes of plasma protoporphyrin as a result of its greater affinity for intracellular liver fatty acid-binding protein.

UI MeSH Term Description Entries
D008099 Liver A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances. Livers
D009363 Neoplasm Proteins Proteins whose abnormal expression (gain or loss) are associated with the development, growth, or progression of NEOPLASMS. Some neoplasm proteins are tumor antigens (ANTIGENS, NEOPLASM), i.e. they induce an immune reaction to their tumor. Many neoplasm proteins have been characterized and are used as tumor markers (BIOMARKERS, TUMOR) when they are detectable in cells and body fluids as monitors for the presence or growth of tumors. Abnormal expression of ONCOGENE PROTEINS is involved in neoplastic transformation, whereas the loss of expression of TUMOR SUPPRESSOR PROTEINS is involved with the loss of growth control and progression of the neoplasm. Proteins, Neoplasm
D009419 Nerve Tissue Proteins Proteins, Nerve Tissue,Tissue Proteins, Nerve
D011166 Porphyrins A group of compounds containing the porphin structure, four pyrrole rings connected by methine bridges in a cyclic configuration to which a variety of side chains are attached. The nature of the side chain is indicated by a prefix, as uroporphyrin, hematoporphyrin, etc. The porphyrins, in combination with iron, form the heme component in biologically significant compounds such as hemoglobin and myoglobin. Porphyrin
D011485 Protein Binding The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. Plasma Protein Binding Capacity,Binding, Protein
D011524 Protoporphyrins Porphyrins with four methyl, two vinyl, and two propionic acid side chains attached to the pyrrole rings. Protoporphyrin IX occurs in hemoglobin, myoglobin, and most of the cytochromes.
D002352 Carrier Proteins Proteins that bind or transport specific substances in the blood, within the cell, or across cell membranes. Binding Proteins,Carrier Protein,Transport Protein,Transport Proteins,Binding Protein,Protein, Carrier,Proteins, Carrier
D003600 Cytosol Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components. Cytosols
D006466 Hemopexin
D000071438 Fatty Acid-Binding Protein 7 A fatty acid-binding protein expressed by ASTROCYTES during CENTRAL NERVOUS SYSTEM development, and by MALIGNANT GLIOMA cells. It is also expressed by ASTROCYTES in response to injury or ISCHEMIA, and may function in repair of the MYELIN SHEATH. Brain Lipid-Binding Protein,Fatty Acid-Binding Protein, Brain,Mammary-Derived Growth Inhibitor Related Protein,Brain Lipid Binding Protein,Fatty Acid Binding Protein 7,Fatty Acid Binding Protein, Brain,Lipid-Binding Protein, Brain,Mammary Derived Growth Inhibitor Related Protein

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