Chapter 2 Reversed-phase and hydrophobic interaction chromatography of carbohydrates and glycoconjugates

Rassi, Ziad El

doi:10.1016/s0301-4770(02)80027-6

Cited by 20 publications

(4 citation statements)

References 349 publications

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“…Over the years, various HPLC methods have been commonly used for glycan purification, including hydrophilic interaction liquid chromatography (HILIC), high-performance anion-exchange chromatography (HPAEC), and reversed-phase chromatography (Ruhaak et al, 2010 ; Nagy et al, 2017 ). HILIC mode HPLC is an efficient technique for separation of unprotected saccharides (Fu et al, 2010 ; Melmer et al, 2011 ; Wan et al, 2015 ) while reversed-phase chromatography is suitable for hydrophobic saccharides (Rajakylä, 1986 ; El Rassi, 1995 ; Dallabernardina et al, 2016 ). HPAEC is usually used for negatively charged unprotected carbohydrates (Rohrer et al, 2013 , 2016 ).…”

Section: Hplc Separation Of Glycans For Functional Studymentioning

confidence: 99%

Preparation of Complex Glycans From Natural Sources for Functional Study

Zhang

Song

2020

Front. Chem.

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One major barrier in glycoscience is the lack of diverse and biomedically relevant complex glycans in sufficient quantities for functional study. Complex glycans from natural sources serve as an important source of these glycans and an alternative to challenging chemoenzymatic synthesis. This review discusses preparation of complex glycans from several classes of glycoconjugates using both enzymatic and chemical release approaches. Novel technologies have been developed to advance the large-scale preparation of complex glycans from natural sources. We also highlight recent approaches and methods developed in functional and fluorescent tagging and high-performance liquid chromatography (HPLC) isolation of released glycans.

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Section: Hplc Separation Of Glycans For Functional Studymentioning

confidence: 99%

Preparation of Complex Glycans From Natural Sources for Functional Study

Zhang

Song

2020

Front. Chem.

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“…Usually two or three columns are used in series or a mixed bed column is employed . In the study of carbohydrates, SEC is used for the determination of the molecular weight distribution of amylose, debranched amylopectin, and enzymatic hydrolysates of starch and cellulose (Nilsson et al, 2001;Rassi, 2002;Nilsson et al, 1996), and for the fractionation of intact starch and cellulose. SEC can be coupled to HPAEC for improved selectivity (Snortti, 1997).…”

Section: Size Exclusion Chromatography (Sec) With Light Scattering Dementioning

confidence: 99%

Profiling of carbohydrate polymers in biotechnology using microdialysis sampling, high performance anion exchange chromatography with integrated pulsed electrochemical detection/mass spectrometry

Okatch¹,

Torto²

2003

Afr. J. Biotechnol.

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The analysis of carbohydrate polymers is very demanding and challenging because of the similar physical and chemical properties they possess. Enzymatic hydrolysis is employed to cleave the polymers. The use of enzymes in analytical chemistry requires an analytical system that has on-line capability, is fast, reproducible, robust, and offers sensitive detection. More importantly the system employed should offer in-situ sampling and sample clean-up so as to reduce the sample handling steps and the analysis time. One such system consists of microdialysis sampling, high performance anion exchange chromatography with integrated pulsed electrochemical detection/mass spectrometry. The on-line system offers sampling, sample clean-up, separation and detection of saccharides as a way of profiling carbohydrate polymers. The wealth of information attained include carbohydrate polymer sequencing, glycosidic linkages, anomericity and result in the unequivocal characterisation of the polymers. This review focuses on the applications of a total on-line system for the profiling of carbohydrate hydrolysates. The above-mentioned analytical system has been employed to carbohydrate polymers and hydrolysates from starch, lignocellulosic material and legumes.

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“…Hydrophobic interaction (HIC) and reversed-phase chromatography (RPLC) are important separation modalities for the purification of proteins (El Rassi et al, 1990;Ingraham, 1991;Shansky et al, 1990;Wu and Karger, 1996). Both of these techniques exploit the hydrophobic or solvophobic nature of the solute (Horvath et al, 1976;Melander and Horvath, 1977).…”

Section: Introductionmentioning

confidence: 99%

Hydrophobic displacement chromatography of proteins

Shukla

Sunasara

Rupp

et al. 2000

Biotechnol. Bioeng.

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Displacement chromatography of proteins was successfully carried out in both hydrophobic interaction and reversed‐phase chromatographic systems using low‐molecular weight displacers. The displacers employed for hydrophobic displacement chromatography were water soluble, charged molecules containing several short alkyl and/or aryl groups. Spectroscopy was employed to verify the absence of structural changes to the proteins displaced on these hydrophobic supports. Displacement chromatography on a reversed‐phase material was employed to purify a growth factor protein from its closely related variants, demonstrating the high resolutions that can be achieved by hydrophobic displacement chromatography. This process combines the high‐resolution/high‐throughput characteristics of displacement chromatography with the unique selectivity of these hydrophobic supports and offers the chromatographic engineer a powerful tool for the preparative purification of proteins. © 2000 John Wiley & Sons, Inc. Biotechnol Bioeng 68: 672–680, 2000.

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Chapter 2 Reversed-phase and hydrophobic interaction chromatography of carbohydrates and glycoconjugates

Cited by 20 publications

References 349 publications

Preparation of Complex Glycans From Natural Sources for Functional Study

Preparation of Complex Glycans From Natural Sources for Functional Study

Profiling of carbohydrate polymers in biotechnology using microdialysis sampling, high performance anion exchange chromatography with integrated pulsed electrochemical detection/mass spectrometry

Hydrophobic displacement chromatography of proteins

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