Gel isoelectric focusing for following the successive carbamylations of amino groups in chymotrypsinogen A
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Cited by (40)
Avenues for post-translational protein modification prevention and therapy
2022, Molecular Aspects of MedicineCitation Excerpt :This disturbance can destabilize secondary and tertiary protein structures resulting in subsequent conformational changes. Dozens of studies have now shown results implicating carbamylation in changes of protein charge (Bobb and Hofstee, 1971; Legendre et al., 1998), conformation (Beswick and Harding, 1987; Monhemi and Tabaee, 2020; Nowicki and Santomé, 1981), and stability (Fazili et al., 1993), with consequent alterations in enzyme and hormone activity (De Furia et al., 1972; Oimomi et al., 1987; Shaw et al., 1964; Van Lente et al., 1986; Veronese et al., 1972), binding properties (Dengler et al., 1992; Lee and Gibson, 1981; Weisgraber et al., 1978), receptor-drug interaction (Erill et al., 1980; Smyth, 1967), and cellular expression and responses (Balion et al., 1998; Garnotel et al., 2004; Ha et al., 2010; Jaisson et al., 2007; Lane and Burka, 1976; Maddock and Westenfelder, 1996). These studies are just a few examples which highlight plausible mechanisms by which hyper-carbamylation could contribute to adverse clinical outcomes.
Post-translational regulation of macrophage migration inhibitory factor: Basis for functional fine-tuning
2018, Redox BiologyCitation Excerpt :The N-terminal proline of MIF has been shown to become carbamylated by the MPO/H2O2/thiocyanate system in vitro (Reaction Scheme 2) [54]. Protein carbamylation was initially identified to be an artefact introduced by denaturation-renaturation, but has since been shown to modulate enzyme activity in different proteins [66,67]. Carbamylation was shown to occur in plasma during uraemia [68–71].
Protein Carbamylation in Chronic Kidney Disease and Dialysis
2018, Advances in Clinical ChemistryCitation Excerpt :With the conformational change of a protein, it is easy to see how functional changes can ensue. Dozens of studies through the years have shown results implicating carbamylation in changes in protein charge [20,21], conformation [19,22], and stability [23], with consequent alterations in enzyme and hormone activity [24–28], binding properties [29–31], receptor-drug interaction [10,32], and cellular expression and responses [33–38]. Descriptions of the numerous demonstrations of these phenomena are beyond the scope of this report and the reader is referred to other excellent broad reviews of carbamylation recently published [4,11].
Eosinophil peroxidase catalyzed protein carbamylation participates in asthma
2016, Journal of Biological ChemistryCitation Excerpt :In end stage renal disease elevated levels of urea lead to enhanced levels of OCN−, and consequently, marked increases in protein carbamylation (37). Nucleophilic groups on proteins such as amino, hydroxyl, or thiol groups may become covalently modified with a carbamyl (NH2CO) group upon exposure to the electrophile OCN−, altering protein primary structure, charge and function, often leading to enzymatic loss of function (38–41). These alterations in structure and charge were first investigated by biochemists studying the reversible denaturation-renaturation of proteins with urea (38–41).
Protein Carbamylation in kidney disease: Pathogenesis and clinical implications
2014, American Journal of Kidney DiseasesCitation Excerpt :Kraus et al20 demonstrated that serum concentrations of many carbamylated free amino acids in patients with ESRD actually exceed the concentrations of their unmodified precursors. A number of studies published over the past several decades have demonstrated that carbamylation causes changes in the physical properties of proteins, thus suggesting its involvement in molecular and cellular dysfunction.6,21 A major chemical effect of carbamylation is neutralization of positively charged lysines, which changes protein-water interactions and alters ionic interactions on the protein surface.12
Improved properties of the non-covalent coating with N,N-didodecyl-N, N-dimethylammonium bromide for the separation of basic proteins by capillary electrophoresis with acidic buffers in 25 μm capillaries
2006, Journal of Chromatography ACitation Excerpt :This would be in accordance with the findings in our studies related above. From studies on electrophoretic mobilities some conclusions can be drawn about the approximate value of the pI in the BGE used (see Fig. 5B), which, as demonstrated (Table 1), are not in accordance with those in literature [47–52]. Our results (Fig. 5B) indicate that the pI-values for all studied proteins are higher in ammonium acetate compared to previously published data (most of them obtained from isoelectric focusing studies).