Immunochemistry of human plasma apolipoprotein C-II as studied by radioimmunoassay

Barr, Susan I.; Kottke, Bruce A.; Chang, Janoi; Mao, Simon J.T.

doi:10.1016/0005-2760(81)90177-6

Cited by 33 publications

(7 citation statements)

References 33 publications

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“…In agreement with other reports, (6)(7)(8), the hypertriglyceridaemic state is accompanied by elevated plasma apolipoprotein C-II concentrations, reaching a 5-to even 10-fold increase in severe Fredrickson type III and type V patients. * * Due to its activating properties on lipoprotein lipase, apolipoprotein C-II plays a key role in the catabolism of the triglyceride-rich lipoproteins.…”

Section: Discussionsupporting

confidence: 91%

“…the assay buffer, no sample pretreatment or additives were used in these apolipoprotein C-II immunoassays. However, Barr et al reported a 73% increase of imnaunoassayable apolipoprotein C-II after plasma delipidation, using a double antibody RIA (8). Similar results were obtained by adding 0.06% Tween 20 to the assay buffer, whereas Triton X-100 did not influence the plasma apolipoprotein C-II concentrations.…”

Section: Discussionmentioning

confidence: 71%

“…These results suggest that Tween 20 might be necessary in order to fully expose the apolipoprotein C-epitopes in the proposed Sandwich ELISA techiqüe. As suggested from the circular dichroism data of Barr et al (8), this detergent might release apolipoprotein C-II from its lipoprotein particle.…”

Section: Discussionmentioning

confidence: 85%

“…Similar results were obtained by adding 0.06% Tween 20 to the assay buffer, whereas Triton X-100 did not influence the plasma apolipoprotein C-II concentrations. Such differences are not readily explained but ßiight originale from the non-standardized use of different antisera äs proposed by Barr et al (8).…”

Section: Discussionmentioning

confidence: 99%

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Human Apolipoprotein C-II Quantitation by Sandwich Enzyme-Linked Immunosorbent Assay

Bury¹,

Michiels²,

Rosseneu³

1986

Clinical Chemistry and Laboratory Medicine

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Summary:A specific, sensitive and accurate, non competitive enzyme-linked immuriosorbent assay was developed for the quantitätion of human apolipoprotein C-II. Using apolipoprotein C-II and apolipoprotein C-III immunosorbent columns, monospecific anti-apolipoprotein C-IFantibodies were prepared for coating and for the preparation of a peroxidase-antibody conjugate. The assay is sensitive down to 0.25 ng apolipoprotein C-II per assay and precise, with mean intra-and inter-assay coefficients of Variation of 3.1% and 7.9% respectively. The apolipoprotein C-II concentrations in normolipaemic and hyperlipaemic plasma were not affected by delipidation, and increased only slightly after treatment with detergents or urea.The mean plasma apolipoprotein C-II concentration in a group of 30 normolipaemic subjects, was 33.1 ± 7.5 mg/1. All hypertriglyceridaemic subjects had significantly elevated apolipoprotein C-II plasma concentrations, which were most pronounced in Fredrickson type III and type V patients.The apolipoprotein C-II profiles, obtained by column fractionation of 6 normolipaemic and 11 hypertriglyceridaemic plasmas, demonstrated a shift of apolipoprotein C-II towards the triglyceride-rich lipoproteins in hypertriglyceridaemic subjects. Bestimmung von Apolipoprotein C-II vom Menschen mit einem Sandwich-Immunosorbent-AssayZusammenfassung: Ein spezifischer, empfindlicher und genauer nicht-kompetitiver Enzyme-Linked-Immunosorbent-Assay wurde für die Quantifizierung von menschlichem Apolipoprotein C-II entwickelt. Mit Apolipoprotein C-II und Apolipoprotein GJII Immunosorbent-Säulen wurden monospezifische anti-Apolipoprotein C-II-Antikörper für die Beschichtung sowie ein Peroxidase-Antikörper-Konjugat hergestellt. Die Empfindlichkeit des Bestimmungsverfahrens beträgt bis zu 0,25 ng Apolipoprotein C-II. Der Assay ist präzis mit mittleren Variationskoeffizienten von 3,1% innerhalb der Serie und 7,9% von Tag zu Tag.Der Apolipoprotein C-II-Gehalt in normolipämischen und hyperlipämischen Plasmen wurde von der Lipidabtrennung nicht beeinflußt und nahm nach Behandlung mit Detergentien oder Harnstoff nur ein wenig zu. Die mittlere Apolipoprotein C-II-Konzentration im Plasma einer Gruppe von 30 normolipämischen Probanden war 33,1 ± 7,5 mg/1. Alle hypertriglyceridämischen Probanden hatten signifikant erhöhte Apolipoprotein C-II Konzentrationen im Plasma, besonders bei Fredrickson Type III und Type V. Die Apolipoprotein C-IIProfile, die durch Saulenfraktionierung von 6 normolipämischen und 11 hypertriglyceridämischen Plasmen erhalten wurden, zeigten eine Verschiebung von Apolipoprotein C-II zu den triglyceridämischen Lipoproteinen in hypertriglyceridämischen Plasmen.

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Section: Discussionsupporting

confidence: 91%

Section: Discussionmentioning

confidence: 71%

Section: Discussionmentioning

confidence: 85%

Section: Discussionmentioning

confidence: 99%

See 2 more Smart Citations

Human Apolipoprotein C-II Quantitation by Sandwich Enzyme-Linked Immunosorbent Assay

Bury¹,

Michiels²,

Rosseneu³

1986

Clinical Chemistry and Laboratory Medicine

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“…Furthermore, a detergent (i.e., Triton X-100) was routinely included in the assay buffer in order to be able to determine PC-transfer protein bound to membrane fractions. Detergents have also been used in radioimmunoassays of, for example, apolipoproteins A-I and C-II in plasma [29,30] and cellular retinol-binding proteins [20,22]. In the presence of Triton X-100, all supernatants, homogenates and subcellular membrane fractions assayed showed displacement curves parallel to the standard curve (see Fig.…”

Section: Partial Hepatectomy 65-75smentioning

confidence: 99%

Tissue distribution and subcellular localization of phosphatidylcholine transfer protein in rats as determined by radioimmunoassay

Teerlink

Krift

Post

et al. 1982

Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metaboli

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A radioimmunoassay for the phosphatidylcholine-transfer protein from rat liver was used to measure levels of PC-transfer protein in rat tissues. The assay as described before (Tee&k, T., Poorthuis, B.J.H.M., Van der Krift, T.P. and Wirtz, K.W.A., Biochim. Biophys. Acta 665 (1981) 74-80) was modified in order to measure PC-transfer protein in tissue homogenates and subcellular membrane fractions. To this end both a detergent (Triton X-100) and a proteolytic enzyme inhibitor (aprotinin) were added to the assay medium. The radioimmunoassay measured levels of PC-transfer protein in the range of 5-50 ng and was specific for PC-transfer protein from rat tissues. Subcellular distribution studies showed that in 10% (w/v) homogenates of liver approximately 60% of the PC-transfer protein was present in the 105000X g supernatant fraction, the remainder being evenly distributed over the particulate fractions. PC-transfer protein associated with the particulate fractions was almost completely removed by a single washing step, suggesting a dynamic equilibrium between membrane-bound and soluble PC-transfer protein. Both 105000X g supematants and homogenates of various rat tissues were assayed. The highest levels of PC-transfer protein were measured in liver and intestinal mucosa. Lower values were found in kidney, spleen and lung, whereas heart and brain contained hardly any PC-transfer protein. PC-transfer protein levels in regenerating rat liver did not differ significantly from levels in normal liver. In fetal lung a change in PC-transfer protein content during development was observed, with a clear maximum 2 days before term, suggesting an involvement of PC-transfer protein in the secretion of lung surfactant.

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Turnover Studies of Apolipoproteins C: A First Critical Appraisal

Malmendier¹,

Lontie²

1989

Recent Developments in Lipid and Lipoprotein Research

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Immunochemistry of human plasma apolipoprotein C-II as studied by radioimmunoassay

Cited by 33 publications

References 33 publications

Human Apolipoprotein C-II Quantitation by Sandwich Enzyme-Linked Immunosorbent Assay

Human Apolipoprotein C-II Quantitation by Sandwich Enzyme-Linked Immunosorbent Assay

Tissue distribution and subcellular localization of phosphatidylcholine transfer protein in rats as determined by radioimmunoassay

Turnover Studies of Apolipoproteins C: A First Critical Appraisal

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