| Literature DB >> 2764887 |
A Gries1, J Nimpf, H Wurm, G M Kostner, T Kenner.
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.Entities:
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Year: 1989 PMID: 2764887 PMCID: PMC1138700 DOI: 10.1042/bj2600531
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857