The Biochemical journal, 407(1), 41-48 (2007-07-26)
Most known organisms encode proteases that are crucial for constitutive proteolytic events. In the present paper, we describe a method to define these events in proteomes from Escherichia coli to humans. The method takes advantage of specific N-terminal biotinylation of
The Journal of dairy research, 49(4), 607-617 (1982-11-01)
Several dicarbonyl compounds (glyoxal, substituted glyoxals, diacetyl and 1, 2-cyclohexanedione) had a marked stabilizing effect on the heat stability of milk, especially in the presence of urea. These reagents are believed to modify arginine more or less specifically suggesting an
Journal of immunology (Baltimore, Md. : 1950), 133(6), 3250-3254 (1984-12-01)
Lysine epsilon-amino groups of human factor H were selectively converted to guanidino groups by treatment with 0.1 M O-methylisourea at pH 10.4. Guanidination resulted in a dose-dependent decrease in the capacity of the regulatory protein to accelerate decay dissociation of
Toxicon : official journal of the International Society on Toxinology, 29(7), 819-826 (1991-01-01)
The effect of modification of amino groups on RTX-III induced lethality in mice has been studied. The toxicity was not affected by guanidination of one or two lysine residues with O-methylisourea, but guanidination of three or four lysine residues decreased
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