The primary structure of the asialo-carbohydrate units of the first glycosylation site of human plasma
Author:
Publisher
Elsevier BV
Subject
Biochemistry, Genetics and Molecular Biology (miscellaneous)
Reference5 articles.
1. The Plasma Proteins;Schmid,1975
2. The carbohydrate units of human plasma α1-Acid glycoprotein
3. Determination of the primary structures of 16 asialo-carbohydrate units derived from human plasma α1-acid glycoprotein by 360-MHz proton NMR spectroscopy and permethylation analysis
4. The structure of the asialo-carbohydrate units of human serotransferrin as proven by 360 MHz proton magnetic resonance spectroscopy
5. Determination by 360 MHZ1H NMR spectroscopy of the type of branching in complex asparagine-linked glycan chains of glycoproteins
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1. The complexity of glycoprotein-derived glycans;Proceedings of the Japan Academy, Series B;2017
2. Characterization of Hepatic Cellular Uptake of α1-Acid Glycoprotein (AGP), Part 2: Involvement of Hemoglobin β-Chain on Plasma Membranes in the Uptake of Human AGP by Liver Parenchymal Cells;Journal of Pharmaceutical Sciences;2012-04
3. Characterization of the Hepatic Cellular Uptake of α1-Acid Glycoprotein (AGP), Part 1: A Peptide Moiety of Human AGP Is Recognized by the Hemoglobin β-Chain on Mouse Liver Parenchymal Cells;Journal of Pharmaceutical Sciences;2012-04
4. Protein Glycosylation: Analysis, Characterization, and Engineering;Encyclopedia of Industrial Biotechnology;2011-05-16
5. Receptor-Mediated Uptake of Human α1-Acid Glycoprotein into Liver Parenchymal Cells in Mice;Drug Metabolism and Pharmacokinetics;2010
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