Detection and Quantification of Carbohydrate-Deficient Transferrin by MALDI-Compatible Protein Chips Prepared by Ambient Ion Soft Landing | Zendy

Petra Darebná | Zendy; Jan Špička | Zendy; Radek Kučera | Zendy; Ondřej Topolčan | Zendy; Eva Navrátilová | Zendy; Viktor Růžička | Zendy; Michael Volný | Zendy; Petr Novák | Zendy; Petr Pompach | Zendy

Open Access

Detection and Quantification of Carbohydrate-Deficient Transferrin by MALDI-Compatible Protein Chips Prepared by Ambient Ion Soft Landing

Author(s) -

Petra Darebná,

Jan Špička,

Radek Kučera,

Ondřej Topolčan,

Eva Navrátilová,

Viktor Růžička,

Michael Volný,

Petr Novák,

Petr Pompach

Publication year - 2018

Publication title -

clinical chemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.705

H-Index - 218

eISSN - 1530-8561

pISSN - 0009-9147

DOI - 10.1373/clinchem.2017.285452

Subject(s) - transferrin , chemistry , chromatography , carbohydrate deficient transferrin , glycosylation , gene isoform , mass spectrometry , biochemistry , alcohol , alcohol consumption , gene

Transferrin is synthetized in the liver and is the most important iron-transport carrier in the human body. Severe alcohol consumption leads to alterations in glycosylation of transferrin. Mass spectrometry can provide fast detection and quantification of transferrin isoforms because they have different molecular masses. In this study, we used antibody chips in combination with MALDI-TOF MS for the detection and quantification of transferrin isoforms.

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