Effects of carbamoylation with alkyl isocyanates on the assay of proteins by dye binding
| Autor: | Michael A. Lea, Aleykutty Luke |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
chemistry.chemical_classification
Aqueous solution Chemistry Metachromasia Proteins Methyl isocyanate Biochemistry Medicinal chemistry Isocyanate chemistry.chemical_compound Spectrophotometry Rosaniline Dyes Methyl orange Organic chemistry Indicators and Reagents Polylysine Coloring Agents Protein carbamoylation Azo Compounds Bradford protein assay Cyanates Alkyl Protein Binding |
| Zdroj: | International Journal of Peptide and Protein Research. 29:561-567 |
| ISSN: | 0367-8377 |
| DOI: | 10.1111/j.1399-3011.1987.tb02285.x |
| Popis: | The effect of carbamoylation with alkyl isocyanate was used both to monitor the stability of the isocyanates and to study the influence of charge modification on protein assay. Carbamoylation of poly (L-lysine) with methyl isocyanate, ethyl isocyanate and 2-chloroethyl isocyanate was observed to decrease binding of methyl orange. The data emphasized the lability of alkyl isocyanates and indicated the importance of preparing aqueous solutions at low temperatures for studies on protein carbamoylation. After carbamoylation of several proteins, there was decreased metachromasia on binding to Coomassie Blue G. Poly (L-lysine) and H1 histone showed anomalous behavior in that with low concentrations of Coomassie Blue G the metachromasia was increased by carbamoylation, but at high concentrations of the dye the metachromasia was decreased by carbamoylation. In contrast to some reports in the literature, the data indicated that there is not always a simple relationship between the positive charge on a protein and the interaction with anionic dyes. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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