The binding of β2-glycoprotein-I to human serum lipoproteins: Distribution among density fractions
Erika Polz,Gerhard M. Kostner +1 more
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It is shown that &GI is present in all major iipoprotein density fractions, especially in chylomicrons, VLDLand HDL, and the highest amount however is found in the bottom fraction of the serum after preparative ultracentrifugation at a solution density of 1.23 g/ml.About:
This article is published in FEBS Letters.The article was published on 1979-06-01 and is currently open access. It has received 227 citations till now. The article focuses on the topics: Very low-density lipoprotein.read more
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beta 2-Glycoprotein I: a plasma inhibitor of the contact activation of the intrinsic blood coagulation pathway.
TL;DR: The present study reports that beta 2-glycoprotein I inhibits the activation of the contact phase system of the intrinsic pathway of blood coagulation.
Journal ArticleDOI
Human plasma protein N-glycosylation
Florent Clerc,Karli R. Reiding,Bas C. Jansen,Guinevere S. M. Kammeijer,Albert Bondt,Manfred Wuhrer,Manfred Wuhrer +6 more
TL;DR: This review aims to convey the current state of knowledge on the N-glycosylation of the major plasma glycoproteins alpha-1-acid glycoprotein, alpha-2-HS-glycop protein, and speculate how the individual proteins may contribute to a total plasma N-behavioural profile determined at the released glycan level.
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Involvement of β2‐glycoprotein I and anticardiolipin antibodies in oxidatively modified low‐density lipoprotein uptake by macrophages
TL;DR: Findings indicate that β2‐GPI may be an anti‐atherogenic protein and that the autoimmune response againstβ2‐ GPI may have a role in the development of atherosclerosis in APS.
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Prothrombinase activity of human platelets is inhibited by β2-glycoprotein-I
J. Nimpf,Edouard M. Bevers,Paul H. H. Bomans,Till U,Helmut Wurm,Gerhard M. Kostner,Robert F. A. Zwaal +6 more
TL;DR: A regulatory role for β 2 -glycoprotein-I is suggested in the pathway of blood coagulation because it causes a reduction of the prothrombinase binding sites of these coagulations factors to platelets or phospholipid vesicles.
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Crystal structure of human β2‐glycoprotein I: implications for phospholipid binding and the antiphospholipid syndrome
Robert Schwarzenbacher,Kornelius Zeth,Kay Diederichs,Anna Gries,Gerhard M. Kostner,Peter Laggner,Ruth Prassl +6 more
TL;DR: The β2GPI structure reveals potential autoantibody‐binding sites and supports mutagenesis studies where Trp316 and CKNKEKKC have been found to be essential for the phospholipid‐binding capacity of β2 GPI.
References
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Estimation of the Concentration of Low-Density Lipoprotein Cholesterol in Plasma, Without Use of the Preparative Ultracentrifuge
TL;DR: A method for estimating the cholesterol content of the serum low-density lipoprotein fraction (Sf0-20) is presented and comparison of this suggested procedure with the more direct procedure, in which the ultracentrifuge is used, yielded correlation coefficients of .94 to .99.
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Apoprotein composition of very low density lipoproteins of human serum.
TL;DR: In this paper, the tetramethylurea was used to delipidates the lipoprotein and selectively precipitates apolipoprotein B. The mean content of apoprotein B in 43 samples from normolipidemic and hyperlipemic subjects was 36.9(+/-1.2 SEM)% of total protein, the distribution of the major soluble apoproteins as mean (+/-SEM) percentage of the soluble fraction was : R-serine, 5.3+/-o.5; arginine-rich, 20.
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Letter: Enzymatic determination of cholesterol in high-density lipoprotein fractions prepared by polyanion precipitation.
TL;DR: Data indicate that more investigations in the area of drug/vitamin A interaction are needed and indicate that four additional drugs influence actual or apparent plasma vitamin A values.
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Charge shift electrophoresis: simple method for distinguishing between amphiphilic and hydrophilic proteins in detergent solution.
Ari Helenius,Kai Simons +1 more
TL;DR: The detergent-induced shift in mobility provides a simple, rapid, and sensitive method for distinguishing between hydrophilic and amphiphilic proteins.