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Заявка 4344868 DB, МКИ G01N 33/96.

Автор(ы) : Vermeer, Hans, Toth, Tibor, Munscher, Gerhard
Заглавие : Verfahren zur Herstellung langzeitstabiler klarer Seren .-
Выходные данные : Б.м.,Б.г.
Коллективы : Behringwerke AG

Вид документа : Статья из журнала

РЖ ВИНИТИ 34 (BI39) 96.04-04К1.61

Автор(ы) : Malle, Ernst, Munscher, Gerhard, Muller, Thomas, Vermeer, Hans, Ibovnik, Anton
Заглавие : Quantification and mapping of antigenic determinants of serum amyloid A (SAA) protein utilizing sequence-specific immunoglobukins and Eu{3+} as a specific probe for time-resolved fluorometric immunoassay
Источник статьи : J. Immunol. Meth. - 1995. - Vol. 182, N 1. - С. 131-144
Аннотация: Serum amyloid A (SAA) protein, the most prominent amongst acute-phase proteins, is the specific precursor protein of secondary reactive amyloidosis. The fact that SAA once released into the circulation as a `free' protein rapidly associates with lipoproteins of the high-density range indicates a specific role in lipoprotein metabolism. In this study a new sensitive assay for quantification of human SAA protein in biological specimens using affinity-purified polyclonal antibodies and Eu{3+} as a specific probe for time-resolved fluorometric immunoassay is presented. Both purified SAA and SAA-rich high-density lipoprotein particles served as reliable standards in the indirect and the direct sandwich dissociation-enhanced lanthanide fluorescence immunoassay (DELFIA). The detection limit of the DELFIA technique presented was 4-10 ng after sample dilution of 1/2500. The intra-assay coefficient of variation averaged 4.3% whereas the inter-assay coefficient of variation averaged 6.2%. Comparison with the nephelometric assay, a widely and commonly used assay for SAA quantification in plasma, revealed correlation coefficients of 0.9428. In addition to polyclonal anti-human SAA antibodies sequence-specific antibodies raised against synthetic peptides corresponding to region; 1-17, 14-30, 27-44, 40-63, 59-72, 68-84, 79-94, and 89-104 of the human SAA amino acid sequence were studied. Sequence-specific antibodies raised against epitopes 27-44, 59-72, 68-84, and 89-104 recognize human SAA protein in the DELFIA assay whereas antibodies raised against epitopes 1-17, 14-30, 40-63 and 79-94 failed to recognize the corresponding epitopes. Results obtained from these studies indicate that the N-terminal domain (1-30) as well as epitopes 40-63 and 79-94 of human SAA are. Австрия, Inst. Med. Biochem., Karl-Franzens Univ., Graz. Библ. 45
ГРНТИ : 34.43.27
Предметные рубрики: СЫВОРОТОЧНЫЙ АМИЛОИД A
АНТИГЕННЫЕ ДЕТЕРМИНАНТЫ
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