Medizinische Universität Graz Austria/Österreich - Forschungsportal - Medical University of Graz
Gewählte Publikation:
Sommer, A; Gorges, R; Kostner, GM; Paltauf, F; Hermetter, A.
Sulfhydryl-selective fluorescence labeling of lipoprotein(a) reveals evidence for one single disulfide linkage between apoproteins(a) and B-100.
Biochemistry. 1991; 30(47):11245-11249
Doi: 10.1021/bi00111a008
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- Co-Autor*innen der Med Uni Graz
- Kostner Gerhard
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- Abstract:
- Human lipoprotein(a) and low-density lipoprotein were labeled with two different sulfhydryl-selective fluorescence markers. The hydrophilic fluorophore lucifer yellow iodoacetamide and the apolar compound 6-acryloyl-2-(dimethylamino)naphthalene were used to derivatize free -SH groups in the lipoproteins. Three sulfhydryls could be detected in low-density lipoprotein, whereas only two cysteines were available in lipoprotein(a). One of the three -SH groups in low-density lipoprotein was shown to be located in close proximity to the particle surface. We suggest that this surface-exposed cysteine of apoprotein B-100 serves as a component for the disulfide linkage to apoprotein(a) in lipoprotein(a).
- Find related publications in this database (using NLM MeSH Indexing)
- 2-Naphthylamine - analogs and derivatives
- Apolipoprotein B-100 - analogs and derivatives
- Apolipoproteins B - blood
- Binding Sites - blood
- Disulfides - analysis
- Humans - analysis
- Isoquinolines - analysis
- Lipoprotein(a) - analysis
- Lipoproteins - blood
- Protein Binding - blood
- Protein Conformation - blood
- Spectrometry, Fluorescence - blood