High-performance liquid chromatography of human glycoprotein hormones

Chlenov, Michael; Kandyba, E. I.; Nagornaya, L. V.; Orlova, Irina L.; Volgin, Yury V.

doi:10.1016/0021-9673(93)80531-c

Cited by 22 publications

(8 citation statements)

References 14 publications

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“…Generally, higher protein recoveries are obtained with shorter and less hydrophobic n-butyl ligands. However, proteins have also been recovered in high yield from n-octadecyl silica in certain applications [22][23][24].…”

Section: Basic Requirements Of Conventional Rplc Stationary Phasesmentioning

confidence: 99%

New trends in reversed-phase liquid chromatographic separations of therapeutic peptides and proteins: Theory and applications

Fekete

Veuthey

Guillarme

2012

Journal of Pharmaceutical and Biomedical Analysis

128

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Section: Basic Requirements Of Conventional Rplc Stationary Phasesmentioning

confidence: 99%

New trends in reversed-phase liquid chromatographic separations of therapeutic peptides and proteins: Theory and applications

Fekete

Veuthey

Guillarme

2012

Journal of Pharmaceutical and Biomedical Analysis

128

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“…At the first stage immunization was performed with a highly purified TSH preparation obtained at the Laboratory of Preparative Chromatography and Ultraffltration of the Institute of Biotechnology [5]. The last two immunizations were performed with preparations from Sigma and from the Research Endocrinological Center of the Russian Academy of Medical Sciences alone or in the form of a complex with T2-8 MAB.…”

Section: Methodsmentioning

confidence: 99%

Preparation of monoclonal antibodies against human thyrotropin suitable for diagnostic systems and their use in clinical practice

et al. 1994

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“…In RPC these effects cause frequently low recovery, band spreading, tailing and multiple peak formation. Nevertheless, a large number of applications of RPC to the determination of proteins can be found in the literature [97,98,99,100].…”

Section: Principlesmentioning

confidence: 99%

Identification, characterization and determination of metal-binding proteins by liquid chromatography. A review

Guntiñas

Bordin

Rodríguez

2002

Analytical and Bioanalytical Chemistry

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The use of liquid chromatography in the separation and determination of metal-binding proteins is reviewed. Advantages and drawbacks of different chromatographic techniques based on various principles: size exclusion, ion exchange (cationic and ionic), reversed phase and affinity, are presented and discussed. The topic "metal-binding proteins" is considered and presented from two different points of view. The first one regards metal speciation in biological samples (serum and blood). In metal speciation studies, the exact identity of the protein to which the metal is bound often remains unknown. The second point of view is that, frequently, the interest of analyzing metal-binding proteins is not related anymore to the metallic fraction of the protein, but to other chemical structures attached to the protein, such as carbohydrates, which indirectly determine how good the function of the protein is. In this review, special attention is paid to studies dealing with the glycosylation of transferrin, and with the glycated isoform of haemoglobin.

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High-performance liquid chromatography of human glycoprotein hormones

Cited by 22 publications

References 14 publications

New trends in reversed-phase liquid chromatographic separations of therapeutic peptides and proteins: Theory and applications

New trends in reversed-phase liquid chromatographic separations of therapeutic peptides and proteins: Theory and applications

Preparation of monoclonal antibodies against human thyrotropin suitable for diagnostic systems and their use in clinical practice

Identification, characterization and determination of metal-binding proteins by liquid chromatography. A review

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