Development of piezoelectric immunosensors for measurement of albuminuria

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F01%3A00004854" target="_blank" >RIV/00216224:14310/01:00004854 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/68378050:_____/01:23010425

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Development of piezoelectric immunosensors for measurement of albuminuria

Popis výsledku v původním jazyce

The development of piezoelectric immunosensors for human serum albumin (HSA) is reported. The piezoelectric crystals were modified either with monoclonal antibody AL-01 (direct assay) or with HSA (competitive assay). Measurements were carried out in theflow-through mode. Affinity interaction between albumin and the antibody was characterised. With immobilised antibody and HSA in solution, the kinetic association rate constant ka was 18100 l mol-1 s-1 and the dissociation constant kd was 0.00369 s-1. For the opposite arrangement (immobilised HSA), a slower dissociation was observed, kd was 0.00085 s-1. A competitive assay for HSA was developed with working range of 1 to 5 ug/ml and a total time for one analysis equal to 17 min. Samples of urine were analysed after tenfold dilution. The developed system was successfully evaluated on real samples from diabetic patients and the obtained results correlated well with the standard reflectometric assay of proteins in urine.

Název v anglickém jazyce

Development of piezoelectric immunosensors for measurement of albuminuria

Popis výsledku anglicky

The development of piezoelectric immunosensors for human serum albumin (HSA) is reported. The piezoelectric crystals were modified either with monoclonal antibody AL-01 (direct assay) or with HSA (competitive assay). Measurements were carried out in theflow-through mode. Affinity interaction between albumin and the antibody was characterised. With immobilised antibody and HSA in solution, the kinetic association rate constant ka was 18100 l mol-1 s-1 and the dissociation constant kd was 0.00369 s-1. For the opposite arrangement (immobilised HSA), a slower dissociation was observed, kd was 0.00085 s-1. A competitive assay for HSA was developed with working range of 1 to 5 ug/ml and a total time for one analysis equal to 17 min. Samples of urine were analysed after tenfold dilution. The developed system was successfully evaluated on real samples from diabetic patients and the obtained results correlated well with the standard reflectometric assay of proteins in urine.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2001

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Talanta

ISSN

0039-9140

e-ISSN

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Svazek periodika

55

Číslo periodika v rámci svazku

11

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

9

Strana od-do

831

Kód UT WoS článku

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EID výsledku v databázi Scopus

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