Journal article


Immunochemical Detection of Oxalic Acid Monoamides which are formed during the Oxidative Reaction of L-Ascorbic Acid and Proteins


Publication Details
Author(s): Pischetsrieder M, Larisch B, Seidel W
Publisher: American Chemical Society
Publication year: 1997
Volume: 45
Pages range: 2070-2075
ISSN: 0021-8561

Abstract

Covalent binding of L-ascorbic acid (AA) to proteins (protein ascorbylation) occurs during food processing and storage and in vivo. It contributes, for example, to browning and various changes in the physical and physiological properties of proteins. Since oxalic acid monoalkylamides (OMAs) are formed in high yields from AA and primary amines under oxidative conditions, it was determined if OMAs also represent an ascorbylation product of proteins. Therefore a polyclonal anti-OMA antibody was raised, and a high-titer antiserum was obtained which is specific against OMA. In a competitive ELISA total binding inhibition was achieved by ascorbylated protein, indicating that ascorbylation of proteins leads to the formation of OMA. OMA is only formed under aerobic conditions. Proteins, which were glycosylated with other carbohydrates such as glucose, did not show cross-reactivity, indicating that the antiserum can be used to detect OMA as a specific marker for ascorbylation.



How to cite
APA: Pischetsrieder, M., Larisch, B., & Seidel, W. (1997). Immunochemical Detection of Oxalic Acid Monoamides which are formed during the Oxidative Reaction of L-Ascorbic Acid and Proteins. Journal of Agricultural and Food Chemistry, 45, 2070-2075. https://dx.doi.org/10.1021/jf960919v

MLA: Pischetsrieder, Monika, Bernd Larisch, and Wolfgang Seidel. "Immunochemical Detection of Oxalic Acid Monoamides which are formed during the Oxidative Reaction of L-Ascorbic Acid and Proteins." Journal of Agricultural and Food Chemistry 45 (1997): 2070-2075.

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