Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P02749 (beta2-glycoprotein I)
 836 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

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.
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PMID:Characterization of isoelectric subspecies of asialo-beta 2-glycoprotein I. 276 87

The binding characteristics of the human serum protein beta 2-glycoprotein-I, also called apolipoprotein H, with multilamellar phospholipid vesicles has been studied. It was found that beta 2-G-I is not or almost not bound to the "neutral" phospholipids phosphatidylcholine (PC), phosphatidylethanolamine (PE) and sphingomyelin (SM). The negatively charged compounds phosphatidylserine (PS) and phosphatidylinositol (PI) interact strongly with beta 2-G-I. In terms of phospholipid concentration the binding to PS is about one order of magnitude greater than to PI. The binding capacity is influenced by several parameters such as the molarity of buffer, presence of mono- or divalent cations as well as ethylenediaminotetraacetic acid (EDTA). Proteins like bovine serum albumin (BSA), human serum albumin (HSA) or horse gamma-globulin (HGG) influence the binding also in a concentration dependent manner.
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PMID:beta 2-Glycoprotein-I (apolipoprotein H) interactions with phospholipid vesicles. 642 35