Obviation of destructive action of 0.2 M NaOH on proteins during arginine modification with cyclohexanedione by use of 0.1 M triethylamine as solvent.
The use of 0.2 M NaOH as a solvent for modification of arginine residues by 1,2-cyclohexanedione in disulfide containing proteins is destructive to the disulfide bonds. Modification can be conveniently done in 0.1 M triethylamine (pH 10.9) without any deleterious effect. Lysozyme was found to retain all its enzymic activity in 0.1 M triethylamine (pH 10.9) whereas complete loss of activity took place in 0.2 M NaOH.
Habeeb
A F
AF
Division of Clinical Immunology and Rheumatology, Department of Medicine and Department of Microbiology, University of Alabama School of Medicine, Birmingham, Ala., USA.
Bennett
J C
JC
D001120:Arginine; D003512:Cyclohexanones; D004220:Disulfides / Q000032:analysis; D005021:Ethylamines; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007074:Immunoglobulin G / Q000737:chemistry; D007202:Indicators and Reagents; D007700:Kinetics; D007768:Lactalbumin / Q000737:chemistry; D009113:Muramidase / Q000737:chemistry* / Q000378:metabolism*; D011506:Proteins / Q000737:chemistry*; D012710:Serum Albumin, Bovine / Q000737:chemistry; D012972:Sodium Hydroxide; D012997:Solvents
D003512:Cyclohexanones; D004220:Disulfides; D005021:Ethylamines; D007074:Immunoglobulin G; D007202:Indicators and Reagents; D011506:Proteins; D012997:Solvents; D012710:Serum Albumin, Bovine; D012972:Sodium Hydroxide; C018031:1,2-cyclohexanedione; D007768:Lactalbumin; D001120:Arginine; D009113:Muramidase; C016162:triethylamine