Human myoglobin: Preparation, quantitation and standardization

Boesken, W. H.; Boesken, Sibylle; Mamier, Anita

doi:10.1007/bf01851590

Cited by 10 publications

(3 citation statements)

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“…Zu (5,8) die Empfindlichkeit der Methode nicht ausreichend, um auch geringe, vermutlich klinisch irrelevante Myoglobinurien (zwischen 0,03 und 0,2 mg/dl) zu erfassen. Versuche durch Konzentrierung der Proben mit Kollodiumhülsen SM 13200 (Sartorius, Göttingen), Myoglobin auch in diesem Bereich mit der radialen Immundiffusion messen zu können, waren leider nicht erfolgreich.…”

Section: Einfache Radiale Immundiffusionunclassified

Nachweis einer Myoglobinurie

Schiwara¹,

Dräger²,

Heitmann³

1981

LaboratoriumsMedizin

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Section: Einfache Radiale Immundiffusionunclassified

Nachweis einer Myoglobinurie

Schiwara¹,

Dräger²,

Heitmann³

1981

LaboratoriumsMedizin

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“…The isolated protein was quantitated by measuring the absorbance at 578 nm (molar extinction coefficient for carbonmonoxy myoglobin is 14.1 mM-' cm-' [2]. Standard stock solution with a myoglobin concentration of 1280 pg/l was prepared in the assay buffer 0.1 molil phosphate buffer, pH 7.4 containing 1.0 g/l bovine serum albumine (AB Kabi) [3]. Further standard solutions were prepared by dilution with the assay buffer.…”

Section: A T E R I a L A N D M E T H O D Smentioning

confidence: 99%

Rapid and sensitive radioimmunoassays for human myoglobin

Hansen

Nørgaard‐Pedersen

1979

Scandinavian Journal of Clinical and Laboratory Investigation

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A radioimmunoassay for quantitation of serum myoglobin in healthy individuals and patients with different diseases is described. Purified myoglobin was labelled by an 125I-labelled ester (N-succinimidyl 3-(-4 hydroxy, 5-[125I]iodophenyl) propionate), a commercially available antiserum was used, and the antigen-antibody complex was precipitated with polyethylene glycol 6000. The rapid assay can be performed within 1 h at 37 degrees C with a detection limit of 45 micrograms/l. Prolonged incubation at 4 degrees C for 18 or 72 h gives a detection limit of 6 and 2 micrograms/l, respectively. The mean coefficient of variation of the routine assay was 11%. In healthy human subjects a significant difference in mean serum myoglobin concentration was found between 43 women (34 +/- 17 micrograms/l) and 51 mean 47 +/- 15 micrograms/l). In twenty patients admitted to hospital with the clinical diagnosis acute myocardial infarction, the serum myoglobin concentration profiles were in close agreement with the final diagnosis. In three patients with myocardial infarction serum samples were taken every 2 h after the acute episode, and serum myoglobin levels were compared with the levels of creatine kinase, lactate dehydrogenase, aspartate aminotransferase and creatine kinase isoenzyme-MB.

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“…These include enzyme linked immunosorbent assay (ELISA) (Sarkara and Mandala, 1985;Alan et al, 1992), and chromatographic (Powell et al, 1984;Mayer et al, 2006;Fresnea, 1964;Han et al, 1994;Maltseva et al, 1987;Kelner and Alexander, 1985) or spectrophotometric methods (Schuder et al, 1979;Modi et al, 1989;Boesken et al, 1977;Shiomi et al, 2005). In general, these methods lack the required specificity and/or involve several steps, are time consuming and require very expensive reagents.…”

Section: Introductionmentioning

confidence: 99%

Myoglobin-biomimetic electroactive materials made by surface molecular imprinting on silica beads and their use as ionophores in polymeric membranes for potentiometric transduction

Moreira

Dutra

Noronha

et al. 2011

Biosensors and Bioelectronics

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Myoglobin (Mb) is among the cardiac biomarkers playing a major role in urgent diagnosis of cardio-vascular diseases. Its monitoring in point-ofcare is therefore fundamental. Pursuing this goal, a novel biomimetic ionophore for the potentiometric transduction of Mb is presented. It was synthesized by surface molecular imprinting (SMI) with the purpose of developing highly efficient sensor layers for near-stereochemical recognition of Mb. The template (Mb) was imprinted on a silane surface that was covalently attached to silica beads by means of self-assembled monolayers. First the silica was modified with an external layer of aldehyde groups. Then, Mb was attached by reaction with its amine groups (on the external surface) and subsequent formation of imine bonds. The vacant places surrounding Mb were filled by polymerization of the silane monomers 3-aminopropyltrimethoxysilane (APTMS) and propy-ltrimethoxysilane (PTMS). Finally, the template was removed by imine cleavage after treatment with oxalic acid. The results materials were finely dispersed in plasticized PVC selective membranes and used as ionophores in potentiometric transduction. The best analytical features were found in HEPES buffer of pH 4. Under this condition, the limits of detection were of 1.3 × 10 −6 mol/L for a linear response after 8.0 × 10 −7 mol/L with an anionic slope of −65.9 mV/decade. The imprinting effect was tested by prepar-ing non-imprinted (NI) particles and employing these materials as ionophores. The resulting membranes showed no ability to detect Mb. Good selectivity was observed towards creatinine, sacarose, fructose, galactose, sodium glutamate, and alanine. The analytical application was conducted successfully and showed accurate and precise results.

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Human myoglobin: Preparation, quantitation and standardization

Cited by 10 publications

References 10 publications

Nachweis einer Myoglobinurie

Nachweis einer Myoglobinurie

Rapid and sensitive radioimmunoassays for human myoglobin

Myoglobin-biomimetic electroactive materials made by surface molecular imprinting on silica beads and their use as ionophores in polymeric membranes for potentiometric transduction

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