PubMed Health⌕ Search
Home/Archive/PubMed

PubMed · 8578541

Pooled patient samples as reference material for D-Dimer.

E Adema·U Gebert
View original source ↗Export metadata ↓

Abstract

A low-D-Dimer concentration has a high negative predictive value for thromboembolic events. Actual and proposed applications include exclusion diagnosis of DIC, DVT and pulmonary embolism (1-7), follow up of cancer therapy (8) and diagnosis of abruptio placentae(9). A variety of tests are commercially available. Unfortunately, due to differences in standardization protocols, the cut-off normal/pathological of one test can usually not be used for another(10). As was shown by Nieuwenhuizen, one way to at least reduce these discrepancies is to use patient material as a reference(11). We have used this approach to standardize the latex test Tinaquant a D-Dimer against the ELISA test Asserachrom D-Dimer.

Explore related subjects

Enzyme-Linked Immunosorbent AssayFibrin Fibrinogen Degradation ProductsFibrinogenHumansReference ValuesThrombosisJournal Article

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

E Adema, U Gebert. 1995-10-01. Pooled patient samples as reference material for D-Dimer.. https://doi.org/10.1016/0049-3848(95)00146-i

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

PubMed2003

Relative quantification of N(epsilon)-(Carboxymethyl)lysine, imidazolone A, and the Amadori product in glycated lysozyme by MALDI-TOF mass spectrometry.

The nonenzymatic glycation of proteins by reducing sugars, also known as the Maillard reaction, has received increasing recognition from nutritional science and medical research. In this study, we applied matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS) to perform relative and simultaneous quantification of the Amadori product, which is an early glycation product, and of N(epsilon)-(carboxymethyl)lysine and imidazolone A, two important advanced glycation end products. Therefore, native lysozyme was incubated with d-glucose for increasing periods of time (1, 4, 8, and 16 weeks) in phosphate-buffered saline pH 7.8 at 50 degrees C. After enzymatic digestion with endoproteinase Glu-C, the N-terminal peptide fragment (m/z 838; amino acid sequence KVFGRCE) and the C-terminal peptide fragment (m/z 1202; amino acid sequence VQAWIRGCRL) were used for relative quantification of the three Maillard products. Amadori product, N(epsilon)-(carboxymethyl)lysine, and imidazolone A were the main glycation products formed under these conditions. Their formation was dependent on glucose concentration and reaction time. The kinetics were similar to those obtained by competitive ELISA, an established method for quantification of N(epsilon)-(carboxymethyl)lysine and imidazolone A. Inhibition experiments showed that coincubation with N(alpha)-acetylargine suppressed formation of imidazolone A but not of the Amadori product or N(epsilon)-(carboxymethyl)lysine. The presence of N(alpha)-acetyllysine resulted in the inhibition of lysine modifications but in higher concentrations of imidazolone A. o-Phenylenediamine decreased the yield of the Amadori product and completely inhibited the formation of N(epsilon)-(carboxymethyl)lysine and imidazolone A. MALDI-TOF-MS proved to be a new analytical tool for the simultaneous, relative quantification of specific products of the Maillard reaction. For the first time, kinetic data of defined products on specific sites of glycated protein could be measured. This characterizes MALDI-TOF-MS as a valuable method for monitoring the Maillard reaction in the course of food processing.

Enzyme-Linked Immunosorbent Assay↗
PubMed2003

Screening for glycosylation changes on recombinant human IgG using lectin methods.

Two lectin-binding methods were investigated as possible ways of monitoring the glycosylation of human monoclonal antibodies during their development and production. Carbohydrate composition was assessed in various preparations that were produced in different host cell types, cell sublines or batches of the same cells. The lectin binding was measured with ELISA and surface plasmon resonance (SPR). For comparative purposes, the monosaccharide content of many of the preparations was also measured by high-pressure anion exchange chromatography (HPAEC)/pulsed amperometric detection (PAD). Both lectin methods detected modifications in glycosylation when antibodies were produced in different ways; SPR was more sensitive than ELISA for some lectins and vice versa. Generally, the lectin results agreed with those obtained by the monosaccharide analysis; however, the former were much better for assessing N -acetylneuraminic acid changes. The latter were impossible to assess by HPAEC/PAD because of their low levels. The lectin-based methods also had the advantages that they were quicker to perform and required less expertise and could quickly identify structures that monosaccharide analysis might miss. It is suggested that, in the development of therapeutic proteins, monosaccharide analysis and/or oligosaccharide profiling is initially performed but later routine batches of the glycoprotein are screened with a lectin method. Of the two lectin methods used, SPR is much quicker when performing a screen, whereas ELISA is particularly useful for comparing a particular carbohydrate feature on different samples of the same glycoprotein.

Enzyme-Linked Immunosorbent Assay↗
PubMed2003

Raised serum interleukin 15 levels in Kawasaki disease.

BACKGROUND: Interleukin (IL)15 is a novel cytokine that induces T cell proliferation, B cell maturation, natural killer cell cytotoxicity, and may have a pivotal role in the pathogenesis of inflammatory disease, acting upstream from tumour necrosis factor alpha (TNFalpha). Kawasaki disease (KD) is an inflammatory disease, in which serum levels of inflammatory cytokines such as TNFalpha and IL6 are increased. OBJECTIVE: To examine the serum levels of IL15 in KD and to evaluate the role of IL15 in estimating the severity of inflammation in KD. RESULTS AND CONCLUSION: There was a significant increase in the mean (SD) serum levels of IL15 measured in the acute stage of KD (11.5 (5.8) pg/ml) compared with those in the subacute stage (1.3 (0.9) pg/ml) (p<0.01) and normal controls (0.9 (1.0) pg/ml) (p<0.01). The increase in IL15 correlated with the increase in TNFalpha (r(s)=0.66, p<0.01); however it did not correlate with the levels of erythrocyte sedimentation rate and C reactive protein, suggesting that IL15 may not be a useful marker in estimating the severity of inflammation in KD.

Enzyme-Linked Immunosorbent Assay↗