Electrochemical assay of protease activities based on polycation/polyanion complex as substrate and polyion sensitive membrane electrode detection

Basit Öğe Kaydı
dc.contributor.authorAbd-Rabboh, Hisham S.M
dc.contributor.authorNevins, Stacey A.
dc.contributor.authorDürüst, Nedime
dc.contributor.authorMeyerhoff, Mark E.
dc.date.accessioned2021-06-23T18:54:50Z
dc.date.available2021-06-23T18:54:50Z
dc.date.issued2002
dc.departmentBAİBÜ, Fen Edebiyat Fakültesi, Kimya Bölümüen_US
dc.description.abstractA novel electrochemical method to detect protease activities is demonstrated. The assay is based on the use of a macromolecular polycation/polyanion substrate; specifically, a complex of the arginine-rich peptide protamine and pentosan polysulfate (PPS), a highly sulfated polysaccharide. As the protease of interest cleaves the protamine within the complex into smaller fragments, free PPS is generated and detected potentiometrically via a polyanion sensitive membrane electrode. Thus, the rate of free PPS generation is proportional to the activity of the protease in the assay solution. The effect of the substrate concentration is examined, as is the influence of the protamine/PPS stoichiometry on the assay performance. Using the optimized composition and concentration of the complex, the determination of trypsin at levels down to 5 U/ml and plasmin at levels approaching 0.002 U/ml can be achieved in a 10 min period. The prospects of further adapting this scheme to determine clot-busting plasminogen activators (e.g. streptokinase, tissue plasminogen activator, etc.) in samples as complex in whole blood are discussed. © 2002 Elsevier Science B.V. All rights reserved.en_US
dc.description.sponsorshipGM28882 Medtronic University of Michigan, U-M Ministry of Higher Education, Egypt, MHEen_US
dc.description.sponsorshipThe authors gratefully acknowledge the National Institute of Health (GM28882) and Medtronic Inc. for financial support of this research. Abd-Rabboh wishes to thank the Ministry of Higher Education of Egypt for supporting his research leave at the University of Michigan.en_US
dc.identifier.doi10.1016/S0956-5663(02)00181-1
dc.identifier.endpage236en_US
dc.identifier.issn0956-5663
dc.identifier.issue2-3en_US
dc.identifier.pmid12485769en_US
dc.identifier.scopus2-s2.0-1842868504en_US
dc.identifier.scopusqualityQ1en_US
dc.identifier.startpage229en_US
dc.identifier.urihttps://doi.org/10.1016/S0956-5663(02)00181-1
dc.identifier.urihttps://hdl.handle.net/20.500.12491/4591
dc.identifier.volume18en_US
dc.indekslendigikaynakScopusen_US
dc.indekslendigikaynakPubMeden_US
dc.institutionauthorDürüst, Nedime
dc.language.isoenen_US
dc.relation.ispartofBiosensors and Bioelectronicsen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectPlasminen_US
dc.subjectPlasminogen activatorsen_US
dc.subjectPolyion sensingen_US
dc.subjectPolymer membrane electrodesen_US
dc.subjectProtease assaysen_US
dc.subjectTrypsinen_US
dc.titleElectrochemical assay of protease activities based on polycation/polyanion complex as substrate and polyion sensitive membrane electrode detectionen_US
dc.typeArticleen_US

Dosyalar

Orijinal paket
Listeleniyor 1 - 1 / 1
Küçük Resim Yok
İsim:
hisham-s.-m.-abd-rabboh.pdf
Boyut:
295.62 KB
Biçim:
Adobe Portable Document Format
Açıklama:
Tam metin/ Full text
İndir

Koleksiyon

Scopus İndeksli Yayınlar Koleksiyonu
Kimya Bölümü Koleksiyonu
PubMed İndeksli Yayınlar Koleksiyonu