Medizinische Universität Graz Austria/Österreich - Forschungsportal - Medical University of Graz
Gewählte Publikation:
Gries, A; Nimpf, J; Wurm, H; Kostner, GM; Kenner, T.
Characterization of isoelectric subspecies of asialo-beta 2-glycoprotein I.
Biochem J. 1989; 260(2):531-534
Doi: 10.1042/bj2600531
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- Führende Autor*innen der Med Uni Graz
- Gries Anna
- Co-Autor*innen der Med Uni Graz
- Kenner Thomas
- Kostner Gerhard
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- Abstract:
- Isoelectric focusing of purified beta 2-glycoprotein I (beta 2-G-I) revealed five major bands with isoelectric points (pI) between 5.1 and 6.1. Neuraminidase treatment decreased the number of bands to two (pI 8.0 and 8.2). The two asialo subfractions of beta 2-G-I were purified by cation-exchange column chromatography. The more basic isoform II was found to have a higher content of lysine. Western-blot analysis of different plasma samples confirmed the heterogeneity of beta 2-G-I in plasma. Plasma treated with neuraminidase showed two bands irrespective of the number of isoforms as well as of the concentration in native plasma. This led us to the conclusion that human plasma beta 2-G-I consists of two isoproteins that are sialylated to different extents.
- Find related publications in this database (using NLM MeSH Indexing)
- Apolipoproteins - isolation and purification
- Blotting, Western - isolation and purification
- Glycoproteins - isolation and purification
- Humans - isolation and purification
- Isoelectric Focusing - isolation and purification
- Isomerism - isolation and purification
- Neuraminidase - isolation and purification
- beta 2-Glycoprotein I - isolation and purification