The binding of porphyrins by ligandin.
Journal: 1978/June - Biochemical Journal
ISSN: 0264-6021
PUBMED: 646788
Abstract:
Spectrophotometric and equilibrium-dialysis measurements show that ligandin (glutathione S-transferase B, EC 2.5.1.18) binds monomeric porphyrins at a single site with association constants in the range 10(4)-10(6) litre/mol at pH 7.0. Binding affinities are paralleled by the tendencies of the porphyrins to aggregate, increasing in the order: uroporphyrins I and III less than coproporphyrins I and III approximately haematoporphyrin less than protoporphyrin IX. From this it is deduced that the hydrophobic effect is the predominant driving-force for binding. The porphyrins can be displaced from their binding site on ligandin by bromosulphophthalein and oestrone sulphate. In enzyme inhibition studies, 50% inhibition was brought about by 8 micron-haematoporphyrin and by 1 micron-protoporphyrin IX. In the analysis of the haemotoporphyrin-ligandin system the self-association of haematoporphyrin was studied in detail. It was found to be limited to dimerization in the concentration range 0-200 micron at pH 7.0, 25 degrees C and a dimerization constant of 1.9 x 10(5) litre/mol was determined. Coproporphrin III has a dimerization constant of 5.2 x 10(5) litre/mol under the same conditions.
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Biochem J 169(3): 509-516

The binding of porphyrins by ligandin.

Abstract

Spectrophotometric and equilibrium-dialysis measurements show that ligandin (glutathione S-transferase B, EC 2.5.1.18) binds monomeric porphyrins at a single site with association constants in the range 10(4)-10(6) litre/mol at pH 7.0. Binding affinities are paralleled by the tendencies of the porphyrins to aggregate, increasing in the order: uroporphyrins I and III less than coproporphyrins I and III approximately haematoporphyrin less than protoporphyrin IX. From this it is deduced that the hydrophobic effect is the predominant driving-force for binding. The porphyrins can be displaced from their binding site on ligandin by bromosulphophthalein and oestrone sulphate. In enzyme inhibition studies, 50% inhibition was brought about by 8 micron-haematoporphyrin and by 1 micron-protoporphyrin IX. In the analysis of the haemotoporphyrin-ligandin system the self-association of haematoporphyrin was studied in detail. It was found to be limited to dimerization in the concentration range 0-200 micron at pH 7.0, 25 degrees C and a dimerization constant of 1.9 x 10(5) litre/mol was determined. Coproporphrin III has a dimerization constant of 5.2 x 10(5) litre/mol under the same conditions.

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  • Brown SB, Shillcock M, Jones P. Equilibrium and kinetic studies of the aggregation of porphyrins in aqueous solution. Biochem J. 1976 Feb 1;153(2):279–285.[PMC free article] [PubMed] [Google Scholar]
  • Gallagher WA, Elliott WB. Ligand-binding in porphyrin systems. Ann N Y Acad Sci. 1973;206:463–482. [PubMed] [Google Scholar]
  • GIBSON QH. THE COMBINATION OF PORPHYRINS WITH NATIVE HUMAN GLOBIN. J Biol Chem. 1964 Oct;239:3282–3287. [PubMed] [Google Scholar]
  • Habig WH, Pabst MJ, Jakoby WB. Glutathione S-transferases. The first enzymatic step in mercapturic acid formation. J Biol Chem. 1974 Nov 25;249(22):7130–7139. [PubMed] [Google Scholar]
  • Kamisaka K, Listowsky I, Arias IM. Circular dichroism studies of Y protein (ligandin), a major organic anion binding protein in liver, kidney, and small intestine. Ann N Y Acad Sci. 1973 Nov 26;226:148–153. [PubMed] [Google Scholar]
  • Kamisaka K, Listowsky I, Gatmaitan Z, Arias IM. Interactions of bilirubin and other ligands with ligandin. Biochemistry. 1975 May 20;14(10):2175–2180. [PubMed] [Google Scholar]
  • Ketley JN, Habig WH, Jakoby WB. Binding of nonsubstrate ligands to the glutathione S-transferases. J Biol Chem. 1975 Nov 25;250(22):8670–8673. [PubMed] [Google Scholar]
  • Ketterer B, Tipping E, Meuwissen J, Beale D. Ligandin. Biochem Soc Trans. 1975;3(5):626–630. [PubMed] [Google Scholar]
  • Ketterer B, Tipping E, Hackney JF, Beale D. A low-molecular-weight protein from rat liver that resembles ligandin in its binding properties. Biochem J. 1976 Jun 1;155(3):511–521.[PMC free article] [PubMed] [Google Scholar]
  • Koskelo P, Toivonen I. Separation of urinary coproporphyrin isomers 1 and 3 by thin-layer chromatography. Studies in healthy subjects and patients with myocardial infarction. Scand J Clin Lab Invest. 1966;18(5):543–549. [PubMed] [Google Scholar]
  • Koskelo P, Toivonen I. Preparation of 14C-labeled series I and 3 porphyrins. Clin Chem. 1970 Jun;16(6):459–461. [PubMed] [Google Scholar]
  • Levi AJ, Gatmaitan Z, Arias IM. Two hepatic cytoplasmic protein fractions, Y and Z, and their possible role in the hepatic uptake of bilirubin, sulfobromophthalein, and other anions. J Clin Invest. 1969 Nov;48(11):2156–2167.[PMC free article] [PubMed] [Google Scholar]
  • Litwack G, Ketterer B, Arias IM. Ligandin: a hepatic protein which binds steroids, bilirubin, carcinogens and a number of exogenous organic anions. Nature. 1971 Dec 24;234(5330):466–467. [PubMed] [Google Scholar]
  • LOWRY OH, ROSEBROUGH NJ, FARR AL, RANDALL RJ. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  • MAEHLY AC. Haemin-protein binding in peroxidase and methaemalbumin. Nature. 1961 Nov 18;192:630–632. [PubMed] [Google Scholar]
  • Meuwissen JA, Ketterer B, Heirwegh KP, de Groote J. Ligandin. Tijdschr Gastroenterol. 1975;18(1):7–20. [PubMed] [Google Scholar]
  • Pasternack RF, Huber PR, Boyd P, Engasser G, Francesconi L, Gibbs E, Fasella P, Venturo GC, Hinds L de C. On the aggregation of meso-substituted water-soluble porphyrins. J Am Chem Soc. 1972 Jun 28;94(13):4511–4517. [PubMed] [Google Scholar]
  • Tipping E, Ketterer B, Christodoulides L, Enderby G. Spectroscopic studies of the binding of bilirubin by ligandin and aminoazo-dye-binding protein A. Biochem J. 1976 Jul 1;157(1):211–216.[PMC free article] [PubMed] [Google Scholar]
  • Tipping E, Ketterer B, Christodoulides L, Enderby G. The interactions of haem with ligandin and aminoazo-dye-binding protein A. Biochem J. 1976 Aug 1;157(2):461–467.[PMC free article] [PubMed] [Google Scholar]
  • Tipping E, Ketterer B, Christodoulides L, Enderby G. The non-convalent binding of small molecules by ligandin. Interactions with steroids and their conjugates, fatty acids, bromosulphophthalein carcinogens, glutathione and realted compounds. Eur J Biochem. 1976 Aug 16;67(2):583–590. [PubMed] [Google Scholar]
  • Woolley PV, 3rd, Hunter MJ, Arias IM. Bilirubin and biliverdin binding to rat Y protein (ligandin). Biochim Biophys Acta. 1976 Sep 28;446(1):115–123. [PubMed] [Google Scholar]
Abstract
Spectrophotometric and equilibrium-dialysis measurements show that ligandin (glutathione S-transferase B, EC 2.5.1.18) binds monomeric porphyrins at a single site with association constants in the range 10(4)-10(6) litre/mol at pH 7.0. Binding affinities are paralleled by the tendencies of the porphyrins to aggregate, increasing in the order: uroporphyrins I and III less than coproporphyrins I and III approximately haematoporphyrin less than protoporphyrin IX. From this it is deduced that the hydrophobic effect is the predominant driving-force for binding. The porphyrins can be displaced from their binding site on ligandin by bromosulphophthalein and oestrone sulphate. In enzyme inhibition studies, 50% inhibition was brought about by 8 micron-haematoporphyrin and by 1 micron-protoporphyrin IX. In the analysis of the haemotoporphyrin-ligandin system the self-association of haematoporphyrin was studied in detail. It was found to be limited to dimerization in the concentration range 0-200 micron at pH 7.0, 25 degrees C and a dimerization constant of 1.9 x 10(5) litre/mol was determined. Coproporphrin III has a dimerization constant of 5.2 x 10(5) litre/mol under the same conditions.
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