Characterization of Covalent Protein Conjugates Using Solid-State 13C NMR Spectroscopy

Joel R. Garbow, Hideji Fujiwara, C. Ray Sharp, Eugene W. Logusch

Research output: Contribution to journalArticle

6 Scopus citations

Abstract

Cross-polarization magic-angle spinning (CPMAS) 13C NMR spectroscopy has been used to characterize covalent conjugates of alachlor, an α-chloroacetamide hapten, with glutathione (GSH) and bovine serum albumin (BSA). The solid-state NMR method demonstrates definitively the covalent nature of these conjugates and can also be used to characterize the sites of hapten attachment to proteins. Three different sites of alachlor binding are observed in the BSA system. Accurate quantitation of the amount of hapten covalently bound to GSH and BSA is reported. The solid-state 13C NMR technique can easily be generalized to study other small molecule/protein conjugates and can be used to assist the development and refinement of synthetic methods needed for the successful formation of such protein alkylation products.

Original languageEnglish
Pages (from-to)7057-7062
Number of pages6
JournalBiochemistry
Volume30
Issue number29
DOIs
StatePublished - Jul 1 1991
Externally publishedYes

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