Stabilization of proteins by guanidination.

P. Cupo, W. El-Deiry, P. L. Whitney, W. M. Awad

Research output: Contribution to journalArticle

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Abstract

Earlier studies have indicated the marked resistance of two pronase endopeptidases to denaturation in high concentrations of urea or guanidine hydrochloride (Siegel, S., and Awad, W. M., Jr. (1973) J. Biol. Chem. 248, 3233--3240). One component has only a single residue of lysine and the other has none. The consideration arose that lysine-containing peptide segments may be less stable than those containing arginine because of the fluctuations of the side groups of the former residue. The small epsilon amino groups may not be able to sustain solvation of the hydrophobic arm in an aqueous medium. Arginine residues have shorter hydrophobic arms, larger hydrophilic groups, and higher pKa values and, thus may be less motile than lysine. The hypothesis was tested by guanidination of seven globular proteins (bovine carbonic anhydrase, chymotrypsinogen, alpha-lactalbumin, serum albumin, ribonuclease, hen egg lysozyme, and horse heart cytochrome c). Conversion of lysine residues to homoarginine was between 90 and 99%. Tritium-hydrogen isotope exchange revealed that all proteins except lysozyme demonstrated reduced out-exchange after guanidination. The results with lysozyme were not unexpected since only this protein has a high arginine to lysine ratio. These findings suggest that high arginine to lysine ratios contribute to protein stability.

Original languageEnglish
Pages (from-to)10828-10833
Number of pages6
JournalJournal of Biological Chemistry
Volume255
Issue number22
StatePublished - Nov 25 1980

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Lysine
Stabilization
Arginine
Proteins
Muramidase
Homoarginine
Chymotrypsinogen
Lactalbumin
Endopeptidases
Pronase
Denaturation
Carbonic Anhydrases
Tritium
Protein Stability
Guanidine
Solvation
Ribonucleases
Cytochromes c
Serum Albumin
Isotopes

ASJC Scopus subject areas

  • Biochemistry

Cite this

Cupo, P., El-Deiry, W., Whitney, P. L., & Awad, W. M. (1980). Stabilization of proteins by guanidination. Journal of Biological Chemistry, 255(22), 10828-10833.

Stabilization of proteins by guanidination. / Cupo, P.; El-Deiry, W.; Whitney, P. L.; Awad, W. M.

In: Journal of Biological Chemistry, Vol. 255, No. 22, 25.11.1980, p. 10828-10833.

Research output: Contribution to journalArticle

Cupo, P, El-Deiry, W, Whitney, PL & Awad, WM 1980, 'Stabilization of proteins by guanidination.', Journal of Biological Chemistry, vol. 255, no. 22, pp. 10828-10833.
Cupo P, El-Deiry W, Whitney PL, Awad WM. Stabilization of proteins by guanidination. Journal of Biological Chemistry. 1980 Nov 25;255(22):10828-10833.
Cupo, P. ; El-Deiry, W. ; Whitney, P. L. ; Awad, W. M. / Stabilization of proteins by guanidination. In: Journal of Biological Chemistry. 1980 ; Vol. 255, No. 22. pp. 10828-10833.
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