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Cross-Reactivity of Polyclonal Antibodies Against Canavalia Ensiformis (Jack Bean) Urease and Helicobacter Pylori Urease Subunit A Fragments

Cross-Reactivity of Polyclonal Antibodies Against Canavalia Ensiformis (Jack Bean) Urease and Helicobacter Pylori Urease Subunit A Fragments

Zbigniew Jerzy Kaminski, Inga Relich, Iwona Konieczna, Wieslaw Kaca, Beata Kolesinska

Chem Biodivers. 2018 Jan;15(1).

PMID: 29156505

Abstract:

Overlapping decapeptide fragments of H. pylori urease subunit A (UreA) were synthesized and tested with polyclonal antibodies against Canavalia ensiformis (Jack bean) urease. The linear epitopes of UreA identified using the dot blot method were then examined using epitope mapping. For this purpose, series of overlapping fragments of UreA, frameshifted ± four amino acid residues were synthesized. Most of the UreA epitopes which reacted with the Jack bean urease polyclonal antibodies had been recognized in previous studies by monoclonal antibodies against H. pylori urease. Fragments 11 - 24, 21 - 33, and 31 - 42 were able to interact with the Jack bean urease antibodies, giving stable immunological complexes. However, the lack of recognition by these antibodies of all the components in the peptide map strongly suggests that a non-continuous (nonlinear) epitope is located on the N-terminal domain of UreA.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP9002135-A	Urease from Canavalia ensiformis (Jack bean)		9002-13-5	Price

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