Characterization of covalent protein conjugates using solid-state sup 13 C NMR spectroscopy

Journal Article · Tue Jul 23 00:00:00 EDT 1991 · Biochemistry; (United States)

DOI:https://doi.org/10.1021/bi00243a004· OSTI ID:5032242

Garbow, J R; Fujiwara, Hideji; Sharp, C R; Logusch, E W ^[1]

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1. Monsanto Co., St. Louis, MO (United States)

Cross-polarization magic-angle spinning (CPMAS) {sup 13}C NMR spectroscopy has been used to characterize covalent conjugates of alachlor, an {alpha}-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 {sup 13}C 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.

• OSTI ID: 5032242
• Journal Information: Biochemistry; (United States), Vol. 30:29; ISSN 0006-2960
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
CHLORINATED ALIPHATIC HYDROCARBONS
NUCLEAR MAGNETIC RESONANCE
GLUTATHIONE CONJUGATES
ACETAMIDE
ALBUMINS
ALKYLATION
CARBON 13
NMR SPECTRA
AMIDES
CARBON ISOTOPES
CHEMICAL REACTIONS
EVEN-ODD NUCLEI
HALOGENATED ALIPHATIC HYDROCARBONS
ISOTOPES
LIGHT NUCLEI
MAGNETIC RESONANCE
METABOLITES
NUCLEI
ORGANIC CHLORINE COMPOUNDS
ORGANIC COMPOUNDS
ORGANIC HALOGEN COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
PROTEINS
RESONANCE
SPECTRA
STABLE ISOTOPES
550201* - Biochemistry- Tracer Techniques