Rapid detection of the main human plasma glycoproteins by two‐dimensional polyacrylamide gel electrophoresis lectin affinoblotting

Golaz, Olivier; Gravel, Patricia; Walzer, Claude; Türler, Hans; Balant, L; Hochstrasser, Denis F.

doi:10.1002/elps.11501601197

Cited by 16 publications

(13 citation statements)

References 15 publications

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“…In red blood cell maps, about 60 spots representing 16 polypeptide chains have been identified so far [15][16][17]. Figure 4 shows the localization of these polypeptide chains on silver stained immobilized pH gradient 2-D PAGE images.…”

Section: Previously Identified Proteinsmentioning

confidence: 99%

“…The reagents and apparatus used have been described in detail by Golaz et al [17] and Hughes et al [23].…”

Section: Reagents and Apparatusmentioning

confidence: 99%

“…The identification of aldehyde dehydrogenase (ALDH) was obtained either by comigration of pure human erythrocyte ALDH with red blood cell total proteins or by immunoblotting using anti-ALDH-antibodies [17] (courtesy of W. Goedde and R. Eckey, Institute of Human Genetics, Hamburg, Germany).…”

Section: Aldehyde Dehydrogenase Identification On Red Blood Cell Mapmentioning

confidence: 99%

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Plasma and red blood cell protein maps: Update 1993

et al. 1993

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This publication updates the reference plasma and red blood cell protein maps obtained with immobilized pH gradients. Seventeen polypeptide spots or chains were partially characterized by direct N-terminal sequencing or by sequencing of peptides obtained from enzymatic digestion. Additional new polypeptides and previously known proteins are listed in a table and/or labeled on the protein maps, thus providing the 1993 update of the human plasma and red blood cell two-dimensional gel SWISS-2DPAGE database. SWISS-2DPAGE and the SWISS-PROT protein sequence databases are closely linked together through the use of common accession numbers.

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Section: Previously Identified Proteinsmentioning

confidence: 99%

“…The reagents and apparatus used have been described in detail by Golaz et al [17] and Hughes et al [23].…”

Section: Reagents and Apparatusmentioning

confidence: 99%

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Plasma and red blood cell protein maps: Update 1993

et al. 1993

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“…An interesting difference is the reactivity of a,-antitrypsin (a,-AT). Up to now no cross-reactivity has been described, neither for this product (19,131; own unpublished data on horse, cow and rat) nor for an As from another company [14].…”

Section: Protein Identificationmentioning

confidence: 99%

Two‐dimensional electrophoresis for the study of blood/serum proteins of the otter, an endangered species

1995

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Studies on serum/blood samples from European otters (Lutra lutra), a species under protection in most countries, were undertaken. Building of a two-dimensional electrophoresis (2-DE) protein identification map was started, identifying serum proteins by pattern comparison with cat or human serum protein maps and by immunoblotting using cross-reacting antibodies against the respective human serum proteins. The capture of endangered species is very restricted, thus making fresh samples almost unavailable; most investigations therefore had to be performed on samples collected from animals found dead. Patterns obtained from specimens of this source were compared to the established pattern of serum proteins and of blood or liver cells. Some of the major differences observed can be explained by contamination with cellular proteins and/or the onset of lytic processes generating breakdown products, as shown by preliminary in vitro experiments. Better knowledge of "normal" serum protein patterns and interfering products will facilitate interpretation of data collected from samples with a less defined history.

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“…8,9 On the other hand, more sensitive and selective methods are needed to understand the function of the lectin in living bodies and to explain the interaction between lectin and sugar in detail. At present, solid-phase assay with an enzyme, 10 method using the avidin-biotin interaction, 11 immunofluorometry 12 and electrophoresis 13 are shown to be useful probes. Although these procedures are sufficient in sensitivity, the separation step contained in them is complicated.…”

Section: Introductionmentioning

confidence: 99%

Voltammetric Detection of Lectin Using Sugar Labeled with Electroactive Substance

et al. 2001

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Lectin, is a protein existing in plants, bacteria and animals. It is known that it contributes to cell control, the aggregation of cell and the formation of organization. Lectin has a property that combines with a sugar residue having a specific structure. The lectin-sugar interaction is related to the membrane receptors of neurotransmitters, hormones and growth factors. [1][2][3] Lectin is also important in medical and clinical fields. 4,5 Therefore, a number of studies concerning the binding between lectin and sugar have been reported. For example, the sugar-binding sites of lectin were determined by affinity chromatography. 6 The affinity constant of lectin-sugar binding was measured by capillary electrophoresis. 7Investigations on the domain of carbohydrate for recognition and the structure of lectin by NMR were also attempted. 8,9 On the other hand, more sensitive and selective methods are needed to understand the function of the lectin in living bodies and to explain the interaction between lectin and sugar in detail. At present, solid-phase assay with an enzyme, 10 method using the avidin-biotin interaction, 11 immunofluorometry 12 and electrophoresis 13 are shown to be useful probes. Although these procedures are sufficient in sensitivity, the separation step contained in them is complicated.Accordingly, the development of a procedure without any separation step is desired. We have already reported a useful electrochemical method used to evaluate the avidin-biotin interaction. It is an advantage of this method that the separation of a free biotin from a bound one is not necessary. 14-16 This procedure will be useful for a rapid evaluation of the concentration of the lectinsugar binding. Based on this background, study that evaluated the lectin-sugar binding by an electrochemical method was first developed by us. In a previous study, a soybean agglutinin (SBA)-galactosamine interaction was reported. 17 The procedure was as follows.Galactosamine and an electroactive daunomycin were combined with a cross-linking reagent (ethylene glyco bis sulfosuccinimidylsuccinate). A sensitive voltammetric measurement was achieved owing to the strong adsorption of daunomycin and a spacer on the electrode. When a part of daunomycin is taken to the binding sites on the basis of the SBA-sugar interaction, the electrode response of daunomycin decreases. Thus, the interaction was evaluated from the change of the electrode response. Generally, it is expected that the peak of the labeled sugar disappears with a sufficient amount of lectin. However, the peak current of daunomycin did not become zero, even if a sufficient amount of lectin that combines to all of the labeled sugar existed. The reason may be that the electroactive part is not perfectly covered with binding sites of the lectin. Consequently, the length of the alkyl chain between sugar and the electroactive part (spacer) for lectin-sugar binding should be investigated.In this study, labeled sugar in which the length of the spacer was shorter was prepared, compared to...

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Rapid detection of the main human plasma glycoproteins by two‐dimensional polyacrylamide gel electrophoresis lectin affinoblotting

Cited by 16 publications

References 15 publications

Plasma and red blood cell protein maps: Update 1993

Plasma and red blood cell protein maps: Update 1993

Two‐dimensional electrophoresis for the study of blood/serum proteins of the otter, an endangered species

Voltammetric Detection of Lectin Using Sugar Labeled with Electroactive Substance

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