Simultaneous measurement of plasma apolipoproteins A-I and B by electroimmunoassay.

1982 ◽  
Vol 28 (1) ◽  
pp. 59-62 ◽  
Author(s):  
J C Fruchart ◽  
I Kora ◽  
C Cachera ◽  
V Clavey ◽  
P Duthilleul ◽  
...  
Keyword(s):  
Simultaneous Measurement ◽  
Apolipoprotein B ◽  
Secondary Standard ◽  
Plastic Film ◽  
Standard Curve ◽  
Atherosclerotic Lesions ◽  
Apolipoprotein A ◽  
Coefficients Of Variation

Abstract We describe a simplified electroimmunoassay for quantification of human apolipoproteins A-I and B on prepared plates. A solution of agarose at 55 degrees C, containing hydroxyethylcellulose and antibodies, is poured onto a plastic film and allowed to gel. Wells are punched in the gels and the plates are dried for storage. Before use, they are rehydrated and buffered. We use succinylated Sudan Black to prestain lipoprotein fractions of plasma. After electrophoresing samples of plasma or standards for 3 h at 4 degrees C at 12.5 V/cm, we measure the peak heights and read the results from a standard curve prepared by using calibrated sera of known apolipoprotein B and A-I content as secondary standard. The within- and between-assay coefficients of variation were less than 4% in all cases. Results correlated well with those obtained by classic electroimmunodiffusion. Subjects with confirmed atherosclerotic lesions had significantly (p less than 10(-9)) lower ratios of apolipoprotein A-I to apolipoprotein B, compared with ratios in controls.

An Improved Method for the Quantitation of Apolipoprotein B and Apolipoprotein A-1 in Dried Blood Spots

1995 ◽  
Vol 32 (2) ◽  
pp. 175-180 ◽  
Author(s):  
N Wong ◽  
J Beeso ◽  
R A Sherwood ◽  
T J Peters
Keyword(s):  
Blood Cells ◽  
Apolipoprotein B ◽  
Dried Blood Spots ◽  
Cross Reactivity ◽  
Deionized Water ◽  
Improved Method ◽  
Apo B ◽  
Blood Spots ◽  
Apolipoprotein A ◽  
Coefficients Of Variation

An extraction protocol has been developed to elute apolipoprotein B (apo B) and apolipoprotein A-1 (apo A-1) from dried blood spots with assay of the extracted apolipoproteins by automated immunoturbidimetry. Various extraction media were investigated to assess their elution efficiency and the optimum medium was found to be deionized water. Studies on the rate of elution suggested both apolipoproteins were eluted readily in less than an hour with a recovery of 71% for apo B and 65% for apo A-1. Extracted apo B but not apo A-1 was found to be stable for 24 h when kept at 4°C. The within-batch coefficients of variation (CV) for the combined extraction and assay of apo B were found to be 5·9% and 8·5% at 0·6 g/L and 1·2 g/L respectively. The CVs for apo A-1 were found to be 7·4% at 0·7 g/L and 8·9% at 1·5 g/L. Antiserum from three sources (Immuno, Incstar and Bayer) was investigated for immunoreactivity with apo B and apo A-1 and cross-reactivity with red blood cells was also assessed. Although the antisera from the three companies showed similar immunoreactivity towards apo B and apo A-1, antiserum from Bayer was found to cross-react with red cells.

scholarly journals The binding of animal low-density lipoproteins to human apolipoprotein(a)

1995 ◽  
Vol 309 (3) ◽  
pp. 899-904 ◽  
Author(s):  
V N Trieu ◽  
W J McConathy
Keyword(s):  
Binding Site ◽  
Apolipoprotein B ◽  
Low Density Lipoproteins ◽  
Low Density ◽  
Covalent Interaction ◽  
Human Apolipoprotein ◽  
Atherosclerotic Lesions ◽  
Apolipoprotein A ◽  
Initial Interaction ◽  
Artery Disease

Lipoprotein(a) [Lp(a)] is a risk factor for coronary artery disease. It is composed of lipids and apolipoprotein(a) [apo(a)] linked to apolipoprotein B (apoB) by a disulphide bond between Cys-4057 of apo(a)'s kringle 36 and possibly Cys-3734 of apoB. We call this the covalent apo(a): apoB-Lp interaction, to distinguish it from the non-covalent apo(a)/Lp(a): apoB-Lp interaction, which is probably mediated by apo(a)'s kringle 33 and residues 3304-3317 of apoB. The non-covalent interaction could be the initial interaction which brings apo(a) and apoB together prior to covalent linkage and Lp(a) formation. The non-covalent apo(a)/Lp(a)-binding site on apoB is evolutionarily more ancient than the covalent apo(a)-binding site on apoB. Both human and non-human low-density lipoproteins (LDLs) bind non-covalently to human apo(a)/Lp(a); however, only rabbit and human LDLs bind covalently to human apo(a). The non-covalent interaction between mouse LDL and human apo(a)/Lp(a) has a Kd of (1.7 +/- 1.33) x 10(-7) M (n = 3). This explains the co-localization of human apo(a) and mouse apoB in the atherosclerotic lesions of human apo(a) transgenic mice and supports our hypothesis that the non-covalent interaction is a contributing factor to apo(a) atherogenicity.

scholarly journals Familial hypertriglyceridemia: an entity with distinguishable features from other causes of hypertriglyceridemia

2021 ◽  
Vol 20 (1) ◽  
Author(s):  
Ivette Cruz-Bautista ◽  
Alicia Huerta-Chagoya ◽  
Hortensia Moreno-Macías ◽  
Rosario Rodríguez-Guillén ◽  
María Luisa Ordóñez-Sánchez ◽  
...  
Keyword(s):  
Apolipoprotein B ◽  
Rare Variants ◽  
Regulatory Proteins ◽  
Fibroblast Growth Factor 21 ◽  
Fibroblast Growth ◽  
Nucleotide Polymorphisms ◽  
Single Nucleotide ◽  
Apo B ◽  
Independent Components ◽  
Apolipoprotein A

Abstract Background Familial hypertriglyceridemia (FHTG) is a partially characterized primary dyslipidemia which is frequently confused with other forms hypertriglyceridemia. The aim of this work is to search for specific features that can help physicians recognize this disease. Methods This study included 84 FHTG cases, 728 subjects with common mild-to-moderate hypertriglyceridemia (CHTG) and 609 normotriglyceridemic controls. All subjects underwent genetic, clinical and biochemical assessments. A set of 53 single nucleotide polymorphisms (SNPs) previously associated with triglycerides levels, as well as 37 rare variants within the five main genes associated with hypertriglyceridemia (i.e. LPL, APOC2, APOA5, LMF1 and GPIHBP1) were analyzed. A panel of endocrine regulatory proteins associated with triglycerides homeostasis were compared between the FHTG and CHTG groups. Results Apolipoprotein B, fibroblast growth factor 21(FGF-21), angiopoietin-like proteins 3 (ANGPTL3) and apolipoprotein A-II concentrations, were independent components of a model to detect FHTG compared with CHTG (AUC 0.948, 95%CI 0.901–0.970, 98.5% sensitivity, 92.2% specificity, P < 0.001). The polygenic set of SNPs, accounted for 1.78% of the variance in triglyceride levels in FHTG and 6.73% in CHTG. Conclusions The clinical and genetic differences observed between FHTG and CHTG supports the notion that FHTG is a unique entity, distinguishable from other causes of hypertriglyceridemia by the higher concentrations of insulin, FGF-21, ANGPTL3, apo A-II and lower levels of apo B. We propose the inclusion of these parameters as useful markers for differentiating FHTG from other causes of hypertriglyceridemia.

scholarly journals Identification of the cysteine residue in apolipoprotein(a) that mediates extracellular coupling with apolipoprotein B-100.

1993 ◽  
Vol 268 (26) ◽  
pp. 19819-19825 ◽  
Author(s):  
M.L. Koschinsky ◽  
G.P. Côté ◽  
B Gabel ◽  
Y.Y. van der Hoek
Keyword(s):  
Apolipoprotein B ◽  
Cysteine Residue ◽  
Apolipoprotein A
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