Preparation of new haptens for use in immunoassay of glycine-conjugated bile acids.

Miyairi, Shinichi; Shioya, Hiroaki; Ebihara, Mitsutaka; Hosoda, Hiroshi; Nambara, Toshio

doi:10.1248/cpb.32.1891

Cited by 6 publications

(2 citation statements)

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“…Several studies have shown that the binding of antibodies is improved when the hapten is separated spatially from the coupling site with a carrier protein such as BSA and keyhole limpet hemocyanin. If the chemical group involved in the linkage between the hapten and the carrier is bound to the recognition site, it is desirable to increase the distance between the steroidal moiety and the carrier protein to increase the probability of raising antibodies with high recognition (29)(30)(31)(32). Accordingly, we designed immunogens in which the terminal carbon of the side chain of LCA was coupled to BSA via a 6-aminohexanoic acid and/ or a succinic acid spacer to produce antibodies specific for the steroid moiety (Fig.…”

Section: Preparation Of Anti-lca Antibodymentioning

confidence: 99%

Immunoprecipitation and MALDI-MS identification of lithocholic acid-tagged proteins in liver of bile duct-ligated rats

Ikegawa

Yamamoto

Ito

et al. 2008

Journal of Lipid Research

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Formation of covalently bound protein adducts with lithocholic acid (LCA) might explain LCAʼs known carcinogenic properties and hepatotoxicity. We performed studies aimed at isolating and identifying hepatic proteins tagged with LCA, presumably via the e-amino group of lysine residues. Antibodies recognizing the 3a-hydroxy-5b-steroid moiety of LCA were generated by immunizing rabbits with immunogens in which the carboxyl group of LCA was coupled to BSA via a 6-aminohexanoic acid and/or succinic acid spacer. The resulting antibodies reacted with N-a-(t-butoxycarbonyl)-L-lysine-e-LCA, the amidated and nonamidated forms of LCA, as well as synthetically prepared LCA adducts with ovalbumin and lysozyme. Proteins tagged with LCA in the liver of bile duct-ligated rats were isolated by immunoprecipitation using these antibodies. Proteins were isolated by two-dimensional electrophoresis, and their structure was identified using matrix-assisted laser desorption ionization time-of-flight mass spectrometry and computerassisted programs. Proteins labeled with LCA were Rab-3, Rab-12, Rab-16, and M-Ras. Rab proteins are Ras-like small GTP binding proteins that regulate vesicle trafficking pathways. The covalent binding of the Rab proteins with LCA may influence vesicular transport or binding of vesicles to their cognate membrane and may contribute to LCA-induced liver toxicity.-Ikegawa, S., T. Yamamoto, H. Ito, S. Ishiwata, T. Sakai, K. Mitamura, and M. Maeda. Immunoprecipitation and MALDI-MS identification of lithocholic acid-tagged proteins in liver of bile duct-ligated rats.

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Section: Preparation Of Anti-lca Antibodymentioning

confidence: 99%

Immunoprecipitation and MALDI-MS identification of lithocholic acid-tagged proteins in liver of bile duct-ligated rats

Ikegawa

Yamamoto

Ito

et al. 2008

Journal of Lipid Research

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“…structure located far from the bridge portion used for conjugation with carrier proteins such as BSA and keyhole limpet hemocyanine (KLH) (12,23,24). Direct condensation through the inherent carboxy group of ibuprofen with a carrier protein is the most convenient way to obtain the immunogen.…”

Section: Figmentioning

confidence: 99%

The Enantioselective Immunoaffinity Extraction of an Optically Active Ibuprofen-Modified Peptide Fragment

Ikegawa

Isriyanthi

Nagata

et al. 2001

Analytical Biochemistry

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ChemInform Abstract: Studies on Steroids. Part 198. Preparation of New Haptens for Use in Immunoassay of Glycine‐Conjugated Bile Acids.

Miyairi¹,

Shioya²,

Hosoda³

et al. 1984

Chemischer Informationsdienst

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Preparation of new haptens for use in immunoassay of glycine-conjugated bile acids.

Cited by 6 publications

References 0 publications

Immunoprecipitation and MALDI-MS identification of lithocholic acid-tagged proteins in liver of bile duct-ligated rats

Immunoprecipitation and MALDI-MS identification of lithocholic acid-tagged proteins in liver of bile duct-ligated rats

The Enantioselective Immunoaffinity Extraction of an Optically Active Ibuprofen-Modified Peptide Fragment

ChemInform Abstract: Studies on Steroids. Part 198. Preparation of New Haptens for Use in Immunoassay of Glycine‐Conjugated Bile Acids.

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