Reversible modification of arginine residues with glyoxal

Journal Article · Wed Mar 29 23:00:00 EST 1978 · Biochem. Biophys. Res. Commun.; (United States)

DOI:https://doi.org/10.1016/0006-291X(78)91566-8· OSTI ID:6790295

Glass, J D; Pelzing, M

Glyoxal reacts with arginine to yield several ninhydrin reactive adducts. One of these, the product favored in strongly acidic solutions, decomposes in the presence of o-phenylenediamine with regeneration of free arginine. Reversible modification of an arginine residue in a peptide has been demonstrated. The conditions for reversibly blocking the guanidino group with glyoxal differ in some respects from those reported for reversible blocking of arginine sidechains with cyclohexanedione. It appears that the two dicarbonyl reagents, glyoxal and cyclohexanedione, might be complementary in their applications to reversible protein modification and to polypeptide semisynthesis.

• Research Organization: Mount Sinai School of Medicine, New York
• OSTI ID: 6790295
• Journal Information: Biochem. Biophys. Res. Commun.; (United States), Journal Name: Biochem. Biophys. Res. Commun.; (United States) Vol. 81:2; ISSN BBRCA
• Country of Publication: United States
• Language: English

Related Subjects

550200* -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
ALDEHYDES
ALKANES
AMINES
AMINO ACIDS
ARGININE
CARBONIC ACID DERIVATIVES
CARBOXYLIC ACIDS
CHEMICAL REACTIONS
CYCLOALKANES
CYCLOHEXANE
DECOMPOSITION
GLYOXAL
GUANIDINES
HYDROCARBONS
KETONES
MODIFICATIONS
NINHYDRIN
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
PEPTIDES
PH VALUE
PHENYLENE RADICALS
POLYPEPTIDES
PROTEINS
RADICALS
REAGENTS
RESIDUES
SYNTHESIS