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#26271987   2015/08/14 Save this To Up

[Preparation and application of monoclonal antibody against human myoglobin].

To prepare the monoclonal antibody (mAb) against human myoglobin (MYO) of high titer and specificity and develop double-antibody sandwich ELISA for detecting MYO in human serum samples.

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#25078431   2014/10/13 Save this To Up

Identification of peptides that selectively bind to myoglobin by biopanning of phage displayed-peptide library.

Biopanning of phage displayed-peptide library was performed against myoglobin, a marker for the early assessment of acute myocardial infarction (AMI), to identify peptides that selectively bind to myoglobin. Using myoglobin-conjugated magnetic beads, phages that bound to myoglobin were collected and amplified for the next round of screening. A 148-fold enrichment of phage titer was observed after five rounds of screening relative to the first round. After phage binding ELISA, three phage clones were selected (3R1, 3R7 and 3R10) and the inserted peptides were chemically synthesized. The analysis of binding affinity showed that the 3R7 (CPSTLGASC) peptide had higher binding affinity (Kd=57 nM) than did the 3R1 (CNLSSSWIC) and 3R10 (CVPRLSAPC) peptide (Kd=125 nM and 293 nM, respectively). Cross binding activity to other proteins, such as bovine serum albumin, troponin I, and creatine kinase-MB, was minimal. In a peptide-antibody sandwich ELISA, the selected peptides efficiently captured myoglobin. Moreover, the concentrations of myoglobin in serum samples measured by a peptide-peptide sandwich assay were comparable to those measured by a commercial antibody-based kit. These results indicate that the identified peptides can be used for the detection of myoglobin and may be a cost effective alternative to antibodies.

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#22652544   2012/08/21 Save this To Up

Serum angiopoietin-like protein 3 concentrations in rheumatic diseases.

Angiopoietin-like protein 3 (Angptl3) is one of the angiogenic cytokines that stimulates endothelial cell adhesion, migration, and neovascularization. No link has been established between Angptl3 and rheumatic diseases such as systemic sclerosis or dermatomyositis (DM). In this study, we determined the serum Angptl3 levels in patients with various rheumatic diseases, and tried to evaluate the possibility that serum levels of Angptl3 can be a useful disease marker. Serum samples were collected from 21 SSc patients, 10 systemic lupus erythematosus (SLE) patients, 21 DM patients, 5 polymyositis (PM) patients and 11 patients with clinically amyopathic DM (CADM) as well as 12 healthy volunteers. Levels of serum Angptl3 were measured with a specific ELISA kit. There was a significant increase of serum Angptl3 levels in patients with SSc or DM (p<0.05). Levels of serum Angptl3 were also slightly higher in patients with ADM, PM or SLE compared with healthy controls, but not statistically significant. Myoglobin levels were significantly higher in DM patients with increased serum Angptl3 levels than those with normal levels (p<0.05). In addition, among patients with SSc, the prevalence of cutaneous ulcers was significantly greater in patients with elevated Angptl3 levels than those with normal levels (p<0.05). Serum Angptl3 levels may be associated with the pathogenesis of muscle involvement in DM patients and microangiopathy in SSc patients. Clarifying the role of Angptl3 in each rheumatic disease may lead to further understanding of the pathogenesis and new therapeutic approaches.

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#10905760   2000/10/25 Save this To Up

Human heart-type cytoplasmic fatty acid-binding protein (H-FABP) for the diagnosis of acute myocardial infarction. Clinical evaluation of H-FABP in comparison with myoglobin and creatine kinase isoenzyme MB.

Heart-type fatty acid-binding protein (H-FABP) is a low molecular weight cytoplasmic protein and present abundantly in the myocardium. When the myocardium is injured, as in the case of myocardial infarction, low molecular weight cytoplasmic proteins including H-FABP are released into the circulation and H-FABP is detectable in a blood sample. We have already developed a direct sandwich-ELISA for quantification of human H-FABP using two distinct types of monoclonal antibodies specific for human H-FABP. In this study we investigated the clinical validity of H-FABP as a biochemical diagnostic marker in the early phase of acute myocardial infarction (AMI). To evaluate the diagnostic usefulness of H-FABP in the early phase of AMI, blood samples were obtained from the following patients within 12 hours after the appearance of symptoms, and serum levels of H-FABP were compared with those of conventional diagnostic markers, such as myoglobin and creatine kinase isoenzyme MB (CK-MB). Blood samples were collected from patients with confirmed AMI (n=140), patients with chest pain who were afterwards not classified as AMI by normal CK-MB levels (non-AMI) (n=49) and normal healthy volunteers (n=75). The serum concentration of H-FABP was quantified with our direct sandwich-ELISA. The concentration of myoglobin mass was measured with a commercial RIA kit. The serum CK-MB activity was determined with an immuno-inhibition assay kit. The overall sensitivity of H-FABP, within 12 hours after the appearance of symptoms, was 92.9%, while it was 88.6% with myoglobin and 18.6% with CK-MB. The overall specificity of H-FABP was 67.3%, while it was 57.1% with myoglobin and 98.0% with CK-MB. The diagnostic efficacy rates with these markers were 86.2% (H-FABP), 80.4% (myoglobin) and 39.2% (CK-MB), respectively. The diagnostic validity of H-FABP was further assessed by receiver operating characteristic (ROC) curve analysis. The area under the curve (AUC) of H-FABP was 0.921, which was significantly greater than with myoglobin (AUC: 0.843) and CK-MB (AUC: 0.654). These parameters, such as sensitivity, specificity, diagnostic efficacy and diagnostic accuracy, obtained for patients with chest pain within 3 hours and/or 6 hours after the onset of symptoms were almost the same as those for patients within 12 hours after symptoms. H-FABP is more sensitive than both myoglobin and CK-MB, more specific than myoglobin for detecting AMI within 12 hours after the onset of symptoms, and shows the highest values for both diagnostic efficacy and ROC curve analysis. Thus, H-FABP has great potential as an excellent biochemical cardiac marker for the diagnosis of AMI in the early phase.

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#9613705   1998/08/03 Save this To Up

Influence of some factors on immunoassays of human myoglobin.

Six ELISA variants exploiting two monoclonal antibodies, one rabbit antibody and their peroxidase conjugates were applied in assays of purified human myoglobin, apomyoglobin and the protein in human muscle extracts. The myoglobin was accurately determined with monoclonal antibody no. 82 used for coating of ELISA plates while assays performed with monoclonal antibody no. 49 or rabbit antibody used for coating were weak or none. Determinations of human apomyoglobin with ELISA variants were somewhat more sensitive than those of myoglobin. Obtained in this work results were compared with those done using commercial Seratec kit for immunoassay of human myoglobin. Addition to the muscle extracts not only concentrated salts but also acetone, ethanol, sodium dodecyl sulfate or some other denaturing agents markedly increased assays of myoglobin by ELISA with monoclonal antibody no. 49 and antibody no. 82 conjugated with peroxidase. Removal of acetone or ammonium sulfate from extracts resulted in dramatic decrease of the estimated myoglobin. Filtration of the extract through Bio-Gel A5m column did not affect low assays of myoglobin in fractions without pretreatment with acetone. Myoglobin was isolated from human heart extract by immunoaffinity chromatography on Sepharose-antibody no. 82 column and the isolated protein was identified by gel electrophoresis and Western blot.

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#7685040   1993/07/08 Save this To Up

The use of T bag synthesis with paper discs as the solid phase in epitope mapping studies.

Epitope mapping with synthetic peptides bound to derivatized paper discs has been investigated using the discs both as a solid-phase matrix for peptide synthesis as well as the solid phase in immunologic testing procedures without detachment of the peptides from the paper discs. Using the T bag (tea bag) method the simultaneous synthesis and subsequent immunologic testing of large numbers of peptides was demonstrated for the feline major allergen Fel d I. A total of 15,000 paper disc-bound peptides, comprising the 146 nonapeptides overlapping by eight amino acid residues on both chains, were synthesized simultaneously with 100 paper discs per T bag. Using these paper disc-bound peptides as the solid phase in radioimmunoassays the binding sites found coincided with those detected in the PEPSCAN with the commercially available epitope mapping kit and with the binding sites that had been found with Sepharose-coupled peptides. The signal to background-ratio in the paper disc-RIA was comparable to that in the PEPSCAN and the reproducibility was good. The bound antibodies could be eluted from the paper disc-bound peptides, permitting regeneration and repeated use of the paper discs for immunologic testing. This method was shown to be a useful alternative to the PEPSCAN and to have the major advantage that large numbers of antibodies could be tested with large numbers of peptides simultaneously.

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#1810699   1992/06/04 Save this To Up

Enzyme immunoassay to determine serum myoglobin in patients with acute myocardial infarction.

A method of "sandwich" enzyme immunoassay was developed for determination of human serum myoglobin with the use of myoglobin isolated from human myocardium and gammaglobulin fraction of a specific sheep antiserum labelled with horseradish peroxidase. The linear part of the calibration curve within the range of 0.08-2.2 nmol/l is suitable for accurate quantitative reading of myoglobin concentration. Intra- and interassay variation coefficients are 7% and 11.2%, respectively. A comparison of 100 serum samples assessed by means of commercially available RIA kit and by the given method revealed a correlation coefficient of 0.86.

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