Dergi makalesi Açık Erişim
Eksin, Ece; Erdem, Arzum
<?xml version='1.0' encoding='utf-8'?>
<resource xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xmlns="http://datacite.org/schema/kernel-4" xsi:schemaLocation="http://datacite.org/schema/kernel-4 http://schema.datacite.org/meta/kernel-4.1/metadata.xsd">
<identifier identifierType="URL">https://aperta.ulakbim.gov.tr/record/77337</identifier>
<creators>
<creator>
<creatorName>Eksin, Ece</creatorName>
<givenName>Ece</givenName>
<familyName>Eksin</familyName>
<affiliation>Ege Univ, Fac Pharm, Dept Analyt Chem, TR-35100 Izmir, Turkey</affiliation>
</creator>
<creator>
<creatorName>Erdem, Arzum</creatorName>
<givenName>Arzum</givenName>
<familyName>Erdem</familyName>
<affiliation>Ege Univ, Fac Pharm, Dept Analyt Chem, TR-35100 Izmir, Turkey</affiliation>
</creator>
</creators>
<titles>
<title>Electrochemical Detection Of N-Homocysteinylated Bsa In The Fetal Bovine Serum Medium</title>
</titles>
<publisher>Aperta</publisher>
<publicationYear>2015</publicationYear>
<dates>
<date dateType="Issued">2015-01-01</date>
</dates>
<resourceType resourceTypeGeneral="Text">Journal article</resourceType>
<alternateIdentifiers>
<alternateIdentifier alternateIdentifierType="url">https://aperta.ulakbim.gov.tr/record/77337</alternateIdentifier>
</alternateIdentifiers>
<relatedIdentifiers>
<relatedIdentifier relatedIdentifierType="DOI" relationType="IsIdenticalTo">10.1039/c4ra13303j</relatedIdentifier>
</relatedIdentifiers>
<rightsList>
<rights rightsURI="http://www.opendefinition.org/licenses/cc-by">Creative Commons Attribution</rights>
<rights rightsURI="info:eu-repo/semantics/openAccess">Open Access</rights>
</rightsList>
<descriptions>
<description descriptionType="Abstract">Homocysteine-thiolactone (HTL) is known as an intramolecular thioester of homocysteine (Hcy). The thioester chemistry of Hcy-thiolactone underlies its ability to form isopeptide bonds with the protein lysine residues, which may impair, or alter the function of protein. HTL modification is a unique post-translational protein modification that is recognized as an emergent biomarker for cardiovascular and neurovascular disease. Electrochemical detection of bovine serum albumin (BSA) before and after N-homocysteinylation was performed using a disposable graphite electrode in combination with a differential pulse voltammetry (DPV) technique. Accordingly, an enhanced detection of BSA was obtained based on the changes at the oxidation signal of BSA after N-homocysteinylation. A lower detection limit was obtained for N-homocysteinylated BSA (N-Hcy-BSA) as 1.09 mu g mL(-1) in comparison to the one of non-homocysteinylated BSA (i.e., 1.55 mu g mL(-1)). The DL of BSA and N-Hcy-BSA in fetal bovine serum medium was also calculated and found to be 3.29 mu g mL(-1) and 2.72 mu g mL(-1), respectively.</description>
</descriptions>
</resource>
| Görüntülenme | 34 |
| İndirme | 7 |
| Veri hacmi | 1.0 kB |
| Tekil görüntülenme | 29 |
| Tekil indirme | 7 |