The DOI matches its Crossref record; 17 of the 17 references it cites were found in a registry or an index.
Labeling of proteins by reductive methylation using sodium cyanoborohydride.
Open accessAbstract
The free amino groups of proteins can be converted to the N,N-dimethyl derivatives by reaction with form-aldehyde and a reducing agent such as NaBH,. The secondary and tertiary amines formed in the reaction retain the charge of the parent amines with only small differences in pK values. Substitution of NaCNBH, (which reduces Schiff bases but not aldehydes) for NaBI& increases labeling efficiency 3-fold and eliminates the side reactions caused by NaB&. In addition, since NaCNBH3 is more stable to acidic conditions, reactions can be carried out at pH values as low as 6 rather than at pH 9 or above as is required when NaBH, is used. Nearly complete conversion of amino groups to the dimethyl derivatives occurs at molar ratios of form-aldehyde to amine of 6 or greater while, at equimolar ratios, as much as 70% of the added formaldehyde is covalently linked to protein. The specificity of the reaction was examined by several methods including studies with model compounds and 13C NMR
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Cites
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Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism
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Metadata
- Authors
- Jentoft, N., & Dearborn, D. G.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1979-06
- Volume
- 254
- Issue
- 11
- Pages
- 4359-4365
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1651280426
- Cited by
- 771
- References
- 17
- FWCI
- 28.37
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Jentoft, N., & Dearborn, D. G. (1979). Labeling of proteins by reductive methylation using sodium cyanoborohydride. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(17)30016-9
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