Kinetics of the interaction of hemin liposomes with heme binding proteins.

As a model for the transport of hemin across biological membranes, sonicated phosphatidylcholine liposomes with incorporated hemin were characterized. The interaction of the hemin liposomes with the heme binding proteins albumin, apomyoglobin, and hemopexin was examined as a function of liposome charge and cholesterol content. In all cases, there was an almost complete transfer of hemin from liposome to protein; a rapid phase and a slow phase were observed for the transfer. For negatively charged liposomes (with 11% dicetyl phosphate), the rapid and slow phases showed observed rates of transfer of ca. 2 and 0.01 s-1, respectively, for all three proteins. The presence of cholesterol in the liposomes decreased the observed rates by a factor of 2, and positively charged liposomes (with 11% stearylamine) showed about one-fifth the observed rates of negatively charged liposomes. The observed rates were independent of protein concentration, indicating that the rate-determining step is hemin efflux from the lipid bilayer. The hemin interaction with the phospholipid bilayer is suggested to be primarily hydrophobic with some electrostatic character. The two phases are suggested to arise from two different populations of hemin within the liposomes and are interpreted as arising from two different orientations of hemin within the bilayer.

[1]  W. Neupert,et al.  Receptor sites involved in posttranslational transport of apocytochrome c into mitochondria: specificity, affinity, and number of sites. , 1983, Proceedings of the National Academy of Sciences of the United States of America.

[2]  H. Ginsburg,et al.  The effect of ferriprotoporphyrin IX and chloroquine on phospholipid monolayers and the possible implications to antimalarial activity. , 1983, Biochimica et biophysica acta.

[3]  T. Williams,et al.  Heterogeneity of albumin as detected by its interactions with deuteroporphyrin IX , 1983 .

[4]  U. Muller-eberhard,et al.  Hemin binding to serum proteins and the catalysis of interprotein transfer. , 1983, Biochemistry.

[5]  Paul Yager,et al.  Encapsulation of hemoglobin in phospholipid vesicles , 1983, FEBS letters.

[6]  Y. Sugita,et al.  Spectral and carbon monoxide binding properties of Fe(II) picket-fence porphyrin and protoheme bound to liposomes. , 1982, Biochemical and biophysical research communications.

[7]  I. Zilber,et al.  The interaction of hemoglobin with phosphatidylserine vesicles. , 1982, Biochimica et biophysica acta.

[8]  U. Muller-eberhard,et al.  The role of cytosolic proteins in the intracellular transport of haem in rat liver. A dual-label approach. , 1982, The Biochemical journal.

[9]  B. Grandchamp,et al.  Formation and disposition of newly synthesized heme in adult rat hepatocytes in primary culture. , 1981, The Journal of biological chemistry.

[10]  W. Morgan,et al.  Hemopexin-mediated transport of heme into isolated rat hepatocytes. , 1981, The Journal of biological chemistry.

[11]  B. Ketterer,et al.  Effect of ligandin on the efflux of Co-deuteroporphyrin from isolated rat liver mitochondria. , 1981, Biochemical and biophysical research communications.

[12]  O. H. Griffith,et al.  Transverse motion of chlorophyll derivatives in phospholipid bilayers. , 1980, Biochimica et biophysica acta.

[13]  P. Adams,et al.  Kinetics and mechanism of the interaction between human serum albumin and monomeric haemin. , 1980, The Biochemical journal.

[14]  U. Müller‐Eberhard,et al.  Effect of hemopexin on the efflux of metalloporphyrin from isolated rat liver mitochondria. , 1980, Biochemical and biophysical research communications.

[15]  D. Barrow,et al.  Large vesicle contamination in small, unilamellar vesicles. , 1980, Biochimica et biophysica acta.

[16]  G. Gregoriadis,et al.  Stability of liposomes in vivo and in vitro is promoted by their cholesterol content and the presence of blood cells. , 1979, Biochemical and biophysical research communications.

[17]  B. Ketterer,et al.  Interactions of small molecules with phospholipid bilayers. Binding to egg phosphatidylcholine of some organic anions (bromosulphophthalein, oestrone sulphate, haem and bilirubin) that bind to ligandin and aminoazo-dye-binding protein A. , 1979, The Biochemical journal.

[18]  B. Kruijff,et al.  Glycophorin facilitates the transbilayer movement of phosphatidylcholine in vesicles. , 1978 .

[19]  R. Hjorth,et al.  The use of wheat-germ lectin-Sepharose for the purification of human haemopexin. , 1977, The Biochemical journal.

[20]  P. Adams.  The kinetics of the recombination reaction between apomyoglobin and alkaline haematin. , 1977, The Biochemical journal.

[21]  F. Roerdink,et al.  Leakage of sucrose from phosphatidylcholine liposomes induced by interaction with serum albumin. , 1977, Biochimica et biophysica acta.

[22]  B. Ketterer,et al.  Haem-binding proteins of the rat liver cytosol. , 1976, Biochimica et biophysica acta.

[23]  Y. Hatefi,et al.  Lipid oxidation in biological membranes. Electron transfer proteins as initiators of lipid autoxidation. , 1975, Archives of biochemistry and biophysics.

[24]  U. Muller-eberhard,et al.  PORPHYRIN‐BINDING PROTEINS IN SERUM * , 1975 .

[25]  Z. Hrkal,et al.  Transfer of heme from ferrihemoglobin and ferrihemoglobin isolated chains to hemopexin. , 1974, European Journal of Biochemistry.

[26]  W. Gratzer,et al.  A spectroscopic study of the haemin--human-serum-albumin system. , 1974, European journal of biochemistry.

[27]  Y. Yip,et al.  Influence of prosthetic groups on protein folding and subunit assembly. I. Conformational differences between separated human alpha- and beta- globins. , 1972, The Journal of biological chemistry.

[28]  J. Simplicio.  Hemin monomers in micellar sodium lauryl sulfate. A spectral and equilibrium study with cyanide. , 1972, Biochemistry.

[29]  B. Yoda,et al.  Transfer of heme from mitochondria in rat liver cells. , 1972, Canadian journal of biochemistry.

[30]  U. Muller-eberhard,et al.  Partial characterization of the heme-binding serum glycoproteins rabbit and human hemopexin. , 1971, Biochemistry.

[31]  U. Muller-eberhard,et al.  Do heme and bilirubin have identical binding sites on the albumin molecule? , 1971, Biochemical and biophysical research communications.

[32]  W. Elliott,et al.  Caffeine derivatives of haematin compounds. , 1967, The Biochemical journal.

[33]  E. Antonini,et al.  Rates of reaction of native human globin with some hemes. , 1963, The Journal of biological chemistry.

[34]  D. Zakim,et al.  Do the soluble glutathione S-transferases have direct access to membrane-bound substrates? , 1983, Biochemical pharmacology.

[35]  S. Granick,et al.  Hemes, chlorophylls, and related compounds: biosynthesis and metabolic regulation. , 1978, Advances in enzymology and related areas of molecular biology.

[36]  A. Swallow,et al.  Pulse radiolysis study of protoferrihaem IX intercalated in sodium dodecyl sulphate micelles , 1978 .

[37]  R. Pasternack,et al.  The interaction of some water-soluble porphyrins and metalloporphyrins with human serum albumin. , 1977, Bioinorganic chemistry.

[38]  S. Provencher.  A Fourier method for the analysis of exponential decay curves. , 1976, Biophysical journal.