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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Wissenschaftlicher Beirat: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred


IMPACT FACTOR 2018: 3.014
5-year IMPACT FACTOR: 3.162

CiteScore 2018: 3.09

SCImago Journal Rank (SJR) 2018: 1.482
Source Normalized Impact per Paper (SNIP) 2018: 0.820

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1437-4315
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Band 382, Heft 2

Hefte

Do Rodent and Human Brains Have Different N-Glycosylation Patterns?

Claus Albach / Roger A. Klein / Brigitte Schmitz
Online erschienen: 01.06.2005 | DOI: https://doi.org/10.1515/BC.2001.026

Abstract

A large number of studies on the structure of Nglycosidically linked oligosaccharides from glycoproteins of different organs and/or different species have been carried out in the past using various combinations of techniques such as monosaccharide analysis, permethylation, peracteylation, exoglycosidase sequencing, normal and reversed phase HPLC, mass spectrometry and nuclear magnetic resonance spectroscopy. Although it is widely accepted that the processing of Nglycans in the ER and Golgi of mammalian cells follows the same principal metabolic rules, analyses have revealed that the glycosylation pattern of a particular protein may differ depending on the cell type in which it is expressed. Nglycans from brain glycoproteins have been shown to include a variety of hybrid and complextype structures with structural features that are not so commonly found on glycoproteins from other organs and which have, therefore, been classified as brainspecific. Comparison of the Nglycans of glycoproteins from homogenates of rat, mouse and human brains confirm that, in general, glycoproteins from human brain show a similar profile of brainspecific Nglycans as glycoproteins from mouse and rat brain.

Artikelinformationen

Online erschienen: 01.06.2005

Erschienen im Druck: 12.02.2001


Quellenangabe: Biological Chemistry, Band 382, Heft 2, Seiten 187–194, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2001.026.

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