Literature DB >> 3827841

Effect of physical environment on the conformation of ricin. Influence of low pH.

J P Frénoy.   

Abstract

The molecular properties of ricin (the toxic lectin from Ricinus communis seeds, RCA II or RCA 60) were evaluated by analytical ultracentrifugation, viscosimetry, c.d., fluorescence and equilibrium dialysis. Measurements of sedimentation (S0(20,W) = 4.60 S) and viscosity (eta = 2.96 X 10(-2) dl/g) indicated that, at neutral pH, the ricin molecule is very compact. Various transitions were explored, and a pH-triggered change in the ricin conformation was observed between pH 7 and 4. In this range, the sedimentation coefficient, far-u.v. c.d. and fluorescence altered simultaneously without unfolding. Below pH 7 the change in the ricin conformation was accompanied by a decrease in the affinity of ricin for galactosides, and at pH 4.0 by an alteration in its binding capacity. These effects of low pH are discussed in relation to the physical conditions encountered by ricin molecules during their entry into living cells.

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Year:  1986        PMID: 3827841      PMCID: PMC1147396          DOI: 10.1042/bj2400221

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  32 in total

1.  Kinetics of binding of the toxic lectins abrin and ricin to surface receptors of human cells.

Authors:  K Sandvig; S Olsnes; A Pihl
Journal:  J Biol Chem       Date:  1976-07-10       Impact factor: 5.157

2.  Circular dichroism and saccharide-induced conformational transitions of lectins from Ricinus communis.

Authors:  K Shimazaki; E F Walborg; G Neri; B Jirgensons
Journal:  Arch Biochem Biophys       Date:  1975-08       Impact factor: 4.013

3.  The ultraviolet fluorescence of proteins. I. The influence of pH and temperature.

Authors:  R F STEINER; H EDELHOCH
Journal:  Biochim Biophys Acta       Date:  1963-05-21

4.  Fluorescence studies with tryptophyl peptides.

Authors:  H Edelhoch; L Brand; M Wilchek
Journal:  Biochemistry       Date:  1967-02       Impact factor: 3.162

Review 5.  Aromatic contributions to circular dichroism spectra of proteins.

Authors:  E H Strickland
Journal:  CRC Crit Rev Biochem       Date:  1974-01

6.  The interaction of Ricinus communis agglutinin with normal and tumor cell surfaces.

Authors:  G L Nicolson; J Blaustein
Journal:  Biochim Biophys Acta       Date:  1972-05-09

7.  Isolation and comparison of galactose-binding lectins from Abrus precatorius and Ricinus communis.

Authors:  S Olsnes; E Saltvedt; A Pihl
Journal:  J Biol Chem       Date:  1974-02-10       Impact factor: 5.157

8.  Abrin and ricin: new anti-tumour substances.

Authors:  J Y Lin; K Y Tserng; C C Chen; L T Lin; T C Tung
Journal:  Nature       Date:  1970-07-18       Impact factor: 49.962

9.  Characterization of two plant lectins from Ricinus communis and their quantitative interaction with a murine lymphoma.

Authors:  G L Nicolson; J Blaustein; M E Etzler
Journal:  Biochemistry       Date:  1974-01-01       Impact factor: 3.162

10.  Studies on the structure and properties of the lectins from Abrus precatorius and Ricinus communis.

Authors:  S Olsnes; K Refsnes; T B Christensen; A Pihl
Journal:  Biochim Biophys Acta       Date:  1975-09-09
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  4 in total

1.  Mechanisms of Ricin Toxin Neutralization Revealed through Engineered Homodimeric and Heterodimeric Camelid Antibodies.

Authors:  Cristina Herrera; Jacqueline M Tremblay; Charles B Shoemaker; Nicholas J Mantis
Journal:  J Biol Chem       Date:  2015-09-22       Impact factor: 5.157

2.  Structure and stability of Ricinus communis haemagglutinin.

Authors:  J P Frénoy; A T Tran; R Bourrillon
Journal:  Biochem J       Date:  1986-11-15       Impact factor: 3.857

3.  Calorimetric studies on the stability of the ribosome-inactivating protein abrin II: effects of pH and ligand binding.

Authors:  J Krupakar; C P Swaminathan; P K Das; A Surolia; S K Podder
Journal:  Biochem J       Date:  1999-03-01       Impact factor: 3.857

4.  Differential neutralizing activities of a single domain camelid antibody (VHH) specific for ricin toxin's binding subunit (RTB).

Authors:  Cristina Herrera; David J Vance; Leslie E Eisele; Charles B Shoemaker; Nicholas J Mantis
Journal:  PLoS One       Date:  2014-06-11       Impact factor: 3.240

  4 in total

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