Immunonephelometry of apolipoprotein A-II in hyperlipoproteinemic serum.

Heuck, C C; Erbe, I; Frech, Kristina; Lohse, P; Münscher, Gerhard

doi:10.1093/clinchem/29.7.1385

Cited by 8 publications

(3 citation statements)

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“…However, tests for the measurement of apolipoproteins have not been used routinely in most clinical laboratories. Apolipoproteins have been measured in clinical laboratories by single radial immunodiffusion method (SRID) (3)(4)(5)(6), radioimmunoassay (RIA) (7), electroimmunoassay (3,4), enzyme immunoassay (8), and immunonephelometry (9)(10)(11)(12)(13)(14). RIA is technically difficult to perform and not easily automated.…”

Section: Introductionmentioning

confidence: 99%

Automated immunoturbidimetric analysis of six plasma apolipoproteins: Correlation with radial immunodiffusion assays

Ikeda

Shibuya

Senba

et al. 1991

Clinical Laboratory Analysis

100

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We measured six apolipoproteins (apo AI, AII, B, CII, CIII, and E) by turbidimetric method using an automatic discrete biochemical analyzer and commercially available antisera. The turbidimetric method was compared with the single radial immunodiffusion method. Linearity for serum apolipoprotein assay by the automated turbidimetric method was better than by the single immuno-diffusion method. The linearity by the turbidimetric method was 2.5 G/L for AI, 1.0 G/L for AII, 4.5 G/L for B, 0.12 G/L for CII, 0.3 G/L for CIII, and 0.12 G/L for E. The presence of high concentrations of bilirubin (up to 0.15 G/L) and hemoglobin (up to 50 G/L) interfered with apolipoprotein measurement. Comparison of the immunoturbidimetric and the single radial immunodiffusion (SRID) methods showed excellent coefficients of correlation, r = 0.963, 0.896, 0.846, 0.936, 0.972, and 0.937 for apo AI, AII, B, CII, CIII, and E, respectively. Reference ranges for the six apolipoproteins were determined by using sera from 450 healthy subjects and were 1.4 +/- 0.3 G/L for AI and 0.3 +/- 0.01 for E. The observed levels of AII (P less than 0.001), B (P less than 0.01), and CIII (P less than 0.01) were significantly higher in males. The serum levels of apo B, CII, and E showed a gradual increase with age which was more prominent in females than in males. The levels of apo AI, AII decreased significantly over an 11 day period in 22 patients with myocardial infarction.

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Section: Introductionmentioning

confidence: 99%

Automated immunoturbidimetric analysis of six plasma apolipoproteins: Correlation with radial immunodiffusion assays

Ikeda

Shibuya

Senba

et al. 1991

Clinical Laboratory Analysis

100

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“…These include their sites of generation , , different interaction capabilities with various plasma factors − , and catabolism . In the context of their heterogeneity, several methods have been used to determine HDL:apolipoprotein stoichiometry, including immunonephelometry , and cross-linking followed by gel-based interpretations . The former method measures scattered light intensity as a function of particle size, and the stoichiometries are then estimated compared to standards with known compositions , .…”

mentioning

confidence: 99%

“…In the context of their heterogeneity, several methods have been used to determine HDL:apolipoprotein stoichiometry, including immunonephelometry , and cross-linking followed by gel-based interpretations . The former method measures scattered light intensity as a function of particle size, and the stoichiometries are then estimated compared to standards with known compositions , . The latter method determines the migration distance of cross-linked HDL particles by sodium dodecyl sulfate−polyacrylamide gel electrophoresis (SDS−PAGE), and the molecular mass ( M r ) determinations of these complexes are conducted with respect to a set of M r standards.…”

mentioning

confidence: 99%

Speciated Human High-Density Lipoprotein Protein Proximity Profiles

Gauthamadasa

Rosales²,

Pownall³

et al. 2010

Biochemistry

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It is expected that the attendant structural heterogeneity of human high density lipoprotein (HDL) complexes is a determinant of its varied metabolic functions. To determine structural heterogeneity of HDL, major apolipoprotein stoichiometry profiles in human HDL were determined. First, HDL was separated into two main populations, with and without apolipoprotein (apo) A-II, LpA-I and LpA-I/A-II respectively. Each main population was further separated into six individual subfractions using size exclusion chromatography (SEC). Protein proximity profiles (PPP) of major apolipoproteins in each individual subfraction was determined by optimally cross-linking apolipoproteins within individual particles with bis(sulfosuccinimidyl)suberate (BS3), a bifunctional cross linker, followed by molecular weight determination by MALDI-MS. The PPPs of LpA-I subfractions indicated that the number of apoA-I molecules increased from two to three to four upon increase in the LpA-I particle size. On the other hand, the entire population of LpA-I/A-II demonstrated the presence of only two proximal apoA-I molecules per particle, while the number of apoA-II molecules varied from one dimeric apoA-II to two and then to three. For most of the above PPP profiles, an additional population that contained a single molecule of apoC-III in addition to apoA-I and/or apoA-II was detected. Upon composition analyses of individual subpopulations, LpA-I/A-II displayed comparable proportions for total protein (~58%), phospholipids (~21%) total cholesterol (~16%), triglycerides (~5%) and free cholesterol (~4%) across subfractions. LpA-I components, on the other hand, showed significant variability. This novel information on HDL subfractions will form a basis for better understanding particle specific functions of HDL.

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Serum A1 and B apolipoprotein determination: comparison of an immunoturbidimetric method with a monoclonal-antibody-based radial immunodiffusion assay

et al. 1992

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Epidemiological and clinical evidence have indicated that apolipoprotein A1 and B determination can better define the lipoprotein pattern in normal subjects and in subjects with coronary heart disease. In this paper, a recent immunoturbidimetric method for routine apolipoprotein A1 and B measurement (using the Turbitimer system and commercially available antisera) has been evaluated. The precision and the accuracy of the method have been previously considered. Within-run and between-run coefficients of variation (ranging from 1.67% to 5.04%) for both assays indicate good precision of the method. Accuracy was evaluated on 2 consecutive days (n = 10 each run) using a standard serum for apolipoprotein A1 and B. The bias obtained was 3.79% for apolipoprotein A1 and 2.30% for B. Apolipoproteins A1 and B were then measured in 100 normal and hyperlipemic sera with the immunoturbidimetric assay and radial immunodiffusion (using the monoclonal antibodies). The data obtained were evaluated by linear regression analysis (Al, r = 0.893; B, r = 0.862). The good correlation between the two methods suggests that the immunoturbidimetric assay can be usefully performed for routine apolipoprotein A1 and B determination because of its lower cost, rapidity, and simplicity.

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Immunonephelometry of apolipoprotein A-II in hyperlipoproteinemic serum.

Cited by 8 publications

References 0 publications

Automated immunoturbidimetric analysis of six plasma apolipoproteins: Correlation with radial immunodiffusion assays

Automated immunoturbidimetric analysis of six plasma apolipoproteins: Correlation with radial immunodiffusion assays

Speciated Human High-Density Lipoprotein Protein Proximity Profiles

Serum A1 and B apolipoprotein determination: comparison of an immunoturbidimetric method with a monoclonal-antibody-based radial immunodiffusion assay

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