Investigations of asialoglycoprotein receptor glycosylation by lectin affinity methods | Zendy

Ivona Baričević | Zendy; Ljiljana Vicovac-Panic | Zendy; Vesna Marinovic | Zendy; Margita Čuperlović | Zendy

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Investigations of asialoglycoprotein receptor glycosylation by lectin affinity methods

Author(s) -

Ivona Baričević,

Ljiljana Vicovac-Panic,

Vesna Marinovic,

Margita Čuperlović

Publication year - 2002

Publication title -

journal of the serbian chemical society

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.227

H-Index - 45

eISSN - 1820-7421

pISSN - 0352-5139

DOI - 10.2298/jsc0205331b

Subject(s) - asialoglycoprotein receptor , lectin , sialic acid , biochemistry , galactose , receptor , chemistry , mannose , glycosylation , microbiology and biotechnology , biology , in vitro , hepatocyte

The asialoglycoprotein receptor belongs to the family of calcium-dependent (C-type) animal lectins. The purified receptor is a glycoprotein in which 10 % of the dry weight consists of sialic acid, galactose, N-acetylglucosamine and mannose. The carbohydrate content of the asialoglycoprotein receptor was investigated by lectin affinity methods. The usefulness of plant lectin affinity methods in the characterization of the saccharide content of the asialoglycoprotein receptor, as an animal lectin, is demonstrated. RCA I, ConA, PHA, SNA I and WGA showed greater affinity toward the asialoglycoprotein receptor, while PSL, AAA and PNA showed negligible interactions with the asialoglycoprotein receptor. The obtained results correlated well with the carbohydrate content of the asialoglycoprotein receptor as determined by chemical methods.

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