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Glycoprotein carbohydrate analytical

Anumula, K.A., and Taylor, P.B. (1992) A comprehensive procedure for preparation of partially methylated alditol acetates from glycoprotein carbohydrates. Analytical Biochemistry, 203,101-108. [Pg.334]

Electrospray mass spectrometry has developed into a well-established method of wide scope and potential over the past 15 years. The softness of electrospray ionization has made this technique an indispensable tool for biochemical and biomedical research. Electrospray ionization has revolutionized the analysis of labile biopolymers, with applications ranging from the analysis of DNA, RNA, oligonucleotides, proteins as well as glycoproteins to carbohydrates, lipids, gly-colipids, and lipopolysaccharides, often in combination with state-of-the-art separation techniques like liquid chromatography or capillary electrophoresis [1,2]. Beyond mere analytical applications, electrospray ionization mass spectrometry (ESMS) has proven to be a powerful tool for collision-induced dissociation (CID) and multiple-stage mass spectrometric (MSn) analysis, and - beyond the elucidation of primary structures - even for the study of noncovalent macromolecular complexes [3]. [Pg.155]

The basic approach of this edition is little changed from the first the emphasis is still on the review of methods and applications which are most useful for quantitative, analytical determination of ions in a wide variety of matrices. An ultimate practitioner of ion chromatography, the author has added a substantial amount of data from his own applications development work. The theoretical background description on various subjects of ion determination is short but informative, and is written so that a novice in the field will not only read and understand it, but also enjoy it. Experts in the field, on the other hand, will undoubtedly find Dr. Weiss s new text a useful reference for many applications and practical problems faced by an analytical chemist, ranging from the field of water purity analysis to the complex task of carbohydrate analysis of glycoproteins. [Pg.471]

Fig. I. Core structures of the carbohydrate units of nervous tissue glycoproteins. The structures are based on analytical data on rat brain glycoproteins and on assumptions of structural similarity with glycan cores from other sources. The main positions of variable or incomplete glycosylation are indicated by arrows. The approximate molar proportions of the glycans in rat brain and the mode of interaction with concanavalin A-Sepharose are indicated (the bisecting GicNAc residue affects the interaction of the diantennary glycans with concanavalin A) [9]. Fig. I. Core structures of the carbohydrate units of nervous tissue glycoproteins. The structures are based on analytical data on rat brain glycoproteins and on assumptions of structural similarity with glycan cores from other sources. The main positions of variable or incomplete glycosylation are indicated by arrows. The approximate molar proportions of the glycans in rat brain and the mode of interaction with concanavalin A-Sepharose are indicated (the bisecting GicNAc residue affects the interaction of the diantennary glycans with concanavalin A) [9].
Anumula KR and Du P (1999) Characterization of carbohydrates using highly fluorescent 2-aminobenzoic acid tag following gel electrophoresis of glycoproteins. Analytical Biochemistry 275 236-242. [Pg.424]


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Carbohydrates glycoproteins

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