Fluorescence polarization analysis of antigen determinant peptides of human fibrinogen

T. Kőszegi, M. Kellermayer, K. Jobst

Research output: Contribution to journalArticle

Abstract

Fluorescamine-labelled human fibrinogen was degraded with trypsin. Using fluorescence detection, the degradation products were fractionated by Sephadex G 50 gel filtration. Fragments of 3000-10,000 molecular weight were isolated for the fluorescence polarization studies. Specific antifibrinogen antibody increased the polarization of the isolated low molecular weight fragments. These results suggest that even the smallest proteolytic fragments of fibrinogen contain antigen determinant sequences. The fluorescence polarization method offers a sensitive and valuable approach for the analysis of the small antigenic peptides of human fibrinogen.

Original languageEnglish
Pages (from-to)169-175
Number of pages7
JournalActa Biochimica et Biophysica Academiae Scientiarum Hungaricae
Volume19
Issue number3-4
Publication statusPublished - 1984

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Fluorescence Polarization
Fibrinogen
Antigens
Peptides
Molecular Weight
Fluorescamine
Trypsin
Gel Chromatography
Fluorescence
Antibodies

ASJC Scopus subject areas

  • Medicine(all)

Cite this

Fluorescence polarization analysis of antigen determinant peptides of human fibrinogen. / Kőszegi, T.; Kellermayer, M.; Jobst, K.

In: Acta Biochimica et Biophysica Academiae Scientiarum Hungaricae, Vol. 19, No. 3-4, 1984, p. 169-175.

Research output: Contribution to journalArticle

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