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Chemical Compound Review

guanidine     guanidine

Synonyms: Guanidin, Imidourea, Iminourea, Carbamidine, Carbamamidine, ...
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Disease relevance of guanidine

  • The proteins of visna are separated into nine major peaks by agarose gel chromatography in 6 M guanidine hydrochloride (GuHCl) [1].
  • This single-chain immunotoxin was expressed in E. coli and purified under denaturing condition of 6M guanidine hydrochloride (GuHCl) [2].

High impact information on guanidine

  • We found that low concentrations of guanidine hydrochloride (GdnHCl, <0.75 M) or urea (<1.5 M) enhanced the enzyme activity of lipocalin-type prostaglandin (PG) D synthase (L-PGDS) maximally 2.5- and 1.6-fold at 0.5 M GdnHCl and 1 M urea, respectively [3].
  • The intensity of the circular dichroism (CD) spectrum at 218 nm, reflecting the beta-sheet content, was also increased by either denaturant in a concentration-dependent manner, with the maximum at 0.5 M GdnHCl or 1 M urea [3].
  • First, provided that the refolding conditions are identical, the two denatured states fold with very similar kinetics, despite the fact the extensive secondary structure is present in the TFE-denatured state but not in the protein denatured in 6 M GuHCl [4].
  • By contrast, binding to chromatin from zone III (containing spermatozoa and little or no detectable receptor) showed no major peak and 4 times less binding at 3 M GuHCl-extracted chromatin [5].
  • In 1 M GdnHCl, the stability of IFN-gamma was greatly reduced and much less protection from HX in solution was observed [6].

Anatomical context of guanidine

  • When PEG was used in the dilution buffer, aggregation of rhDNAse did not occur during refolding in either case. rhtPA produced from CHO cells was denatured in 5 M guanidine hydrochloride (GuHCl) and refolded by rapid dilution to 0.10 M GuHCl and 0.20 mg/ml protein.(ABSTRACT TRUNCATED AT 250 WORDS)[7]

Associations of guanidine with other chemical compounds

  • These results show that helix C, which forms the hydrophobic core of the IFN-gamma dimer, is highly protected from HX under native conditions, is more stable in GdnHCl than the rest of the protein and remains intact in both GdnHCl- and KSCN-induced aggregates [6].
  • Previous folding studies of alpha-1-proteinase inhibitor (alpha1-PI), which regulates the activity of the serine protease human neutrophil elastase, show an intermediate state at approximately 1.5 M guanidine-HCl (Gu) [8].

Gene context of guanidine

  • By plotting the enzyme activities against the ellipticities at 218 nm of the CD spectra of L-PGDS in the presence or absence of GdnHCl or urea, we found two states in the reversible folding process of L-PGDS: one is an activity-enhanced state and the other, an inactive state [3].
  • Citrate synthase (CS), which has been denatured in either guanidine hydrochloride (GdnHCl) or urea can be assisted in its renaturation in a variety of ways [9].
  • From kinetic unfolding experiments in 5 M GdnHCl it was determined that the conversion of M1 to M2 had an activation energy of 26.5 kcal/mol, a half-life of 23 h at 25 degrees C, and the rate of formation of M2 was dependent on the GdnHCl concentration between 5 and 7.1 M GdnHCl [10].

Analytical, diagnostic and therapeutic context of guanidine


  1. Polyacrylamide gel electrophoresis of visna virus polypeptides isolated by agarose gel chromatography. Lin, F.H. J. Virol. (1978) [Pubmed]
  2. Expression and purification of recombinant immunotoxin--a fusion protein stabilizes a single-chain Fv (scFv) in denaturing condition. Kim, S.H. Protein Expr. Purif. (2003) [Pubmed]
  3. Characterization of the unfolding process of lipocalin-type prostaglandin D synthase. Inui, T., Ohkubo, T., Emi, M., Irikura, D., Hayaishi, O., Urade, Y. J. Biol. Chem. (2003) [Pubmed]
  4. Acceleration of the folding of hen lysozyme by trifluoroethanol. Lu, H., Buck, M., Radford, S.E., Dobson, C.M. J. Mol. Biol. (1997) [Pubmed]
  5. Tissue and species specificity of unmasked nuclear acceptor sites for the estrogen receptor of Squalus testes. Ruh, M.F., Singh, R.K., Mak, P., Callard, G.V. Endocrinology (1986) [Pubmed]
  6. Structural features of interferon-gamma aggregation revealed by hydrogen exchange. Tobler, S.A., Fernandez, E.J. Protein Sci. (2002) [Pubmed]
  7. Polyethylene glycol enhanced protein refolding. Cleland, J.L., Builder, S.E., Swartz, J.R., Winkler, M., Chang, J.Y., Wang, D.I. Biotechnology (N.Y.) (1992) [Pubmed]
  8. The folding of alpha-1-proteinase inhibitor: kinetic vs equilibrium control. Tran, S.T., Shrake, A. Arch. Biochem. Biophys. (2001) [Pubmed]
  9. Renaturation of citrate synthase: influence of denaturant and folding assistants. Zhi, W., Landry, S.J., Gierasch, L.M., Srere, P.A. Protein Sci. (1992) [Pubmed]
  10. RhNGF slow unfolding is not due to proline isomerization: possibility of a cystine knot loop-threading mechanism. De Young, L.R., Burton, L.E., Liu, J., Powell, M.F., Schmelzer, C.H., Skelton, N.J. Protein Sci. (1996) [Pubmed]
  11. Equilibrium and kinetic folding of rabbit muscle triosephosphate isomerase by hydrogen exchange mass spectrometry. Pan, H., Raza, A.S., Smith, D.L. J. Mol. Biol. (2004) [Pubmed]
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