Fractionation and Structural Assessment of Oligosaccharides and Glycopeptides by Use of Immobilized Lectins

Osawa, Tatsushi; Tsuji, Takashi

doi:10.1146/annurev.bi.56.070187.000321

Cited by 318 publications

(138 citation statements)

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“…The biochemical characteristics of WGP-88 were compared with those of P AS-4, the interaction with lectins providing information on the sugar chain of WGP-88. Its high affinity to Con A, PHA-E4, PNA, RCA-120, and WFA 38,39) suggests that WGP-88 had N-and O-linked sugar chains, in agreement with the results from reductive hydrolysis and N-glycanase (Table III). The molecular mass of 78 kDa for PAS-4 and of 88 kDa for WGP-88 were decreased to 57 kDa after deglycosylating with N-glycanase.…”

Section: Discussionsupporting

confidence: 84%

Purification and Characterization of Novel Whey Glycoprotein WGP-88 Which Binds to a Monoclonal Antibody to PAS-4 Glycoprotein in the Bovine Milk Fat Globule Membrane

Hwangbo

Azuma

Kurisaki

et al. 1997

Bioscience, Biotechnology, and Biochemistry

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Section: Discussionsupporting

confidence: 84%

Purification and Characterization of Novel Whey Glycoprotein WGP-88 Which Binds to a Monoclonal Antibody to PAS-4 Glycoprotein in the Bovine Milk Fat Globule Membrane

Hwangbo

Azuma

Kurisaki

et al. 1997

Bioscience, Biotechnology, and Biochemistry

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“…EPO is rich in core fucosylated tetraantennary oligosaccharides [24], and WGA is expected to bind to the terminal parts of the carbohydrate structures, especially the protruding polylactosamine structures [25]. Such structures are much more common in rhEPO than in endogenous EPO [24].…”

Section: Discussionmentioning

confidence: 99%

Patients with anaemia can shift from kidney to liver production of erythropoietin as shown by glycoform analysis

Lönnberg

Garle

Lönnberg

et al. 2013

Journal of Pharmaceutical and Biomedical Analysis

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The primary production site of erythropoietin (EPO) is shifted from the liver to the kidney shortly after birth. Under conditions of lost or reduced kidney production, it is valuable to measure the production capacity of the liver. However, there is a lack of urine or serum based methods that can distinguish endogenous EPO produced in different cell types. Here is presented a method based on chromatographic interaction with the lectin wheat germ agglutinin (WGA) that can distinguish presumably liver-produced EPO, found in anaemic patients receiving epoetin and darbepoetin, from kidney-produced EPO found in healthy individuals.All the tested samples from haemodialysis patients with end-stage renal disease showed a presence of liver EPO. In some samples, the liver-produced EPO made up 90-100% of total EPO at a concentration of 8-10 ng/L in urine, which indicates that the liver has a quite high production capacity, although not adequate for the degree of anaemia.This glycoform analysis has made it possible to affirm that some anaemic patients can increase their liver-production of EPO. The use of such a method can give better insight into the regulation of non-renal endogenous EPO production, a potential source of EPO intended to replace administration of exogenous EPO.

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“…In considering such binding specificity, it is concluded that the sugar moiety of the CDF is composed of mannose and/or galactose, as inferred from Osawa and Tsuji (1987) and Cummings (1994). Regarding the role of sugar moiety of the CDF, its presence is required for the induction of cell division of the auxin-starved BY-2 cells, since the enzymatic removal of the sugar moiety eliminated its biological activity (Shimizu et al 2006).…”

Section: Discussionmentioning

confidence: 99%

“…On the other hand, the CDF simply passed through the column in the case of agarose column binds to PHA-E 4 , PHA-L 4 and UEA-I. In considering such binding specificities of the CDF to certain types of lectins, it is concluded that major portions of the sugar moiety of the CDF are composed of mannose and/or galactose (Osawa andTsuji 1987, Cummings 1994).…”

Section: Binding Characteristics Of Cdf To Lectinsmentioning

confidence: 99%

Characterization of Sugar Moieties of a Cell Division Factor from Tobacco 2B-13 Cells

Shimizu

Nagata

2006

CYTOLOGIA

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Summary A cell division-inducing factor (CDF) purified from the culture filtrates of auxin autotrophic 2B-13 cells induced semi-synchronous cell division in auxin-starved tobacco BY-2 cells. The CDF was identified as a glycoprotein, whose polypeptide chains have been found to have homology to ATP-binding cassette (ABC) transporters, while its sugar moiety has not yet been characterized. Specific binding of the CDF to several types of lectins suggests that the sugar moiety of the CDF is composed of mannose and/or galactose. Furthermore, specific binding of the CDF to b-glucosyl Yariv reagent suggests that the CDF has certain characteristics of arabinogalactan proteins. Intriguingly, the addition of increased amounts of b-glucosyl Yariv reagent to the culture medium inhibited 2,4-D induced cell division of auxin-starved BY-2 cells, suggesting that the CDF plays a pivotal role in inducing cell division in the auxin signaling pathways.

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Fractionation and Structural Assessment of Oligosaccharides and Glycopeptides by Use of Immobilized Lectins

Cited by 318 publications

References 0 publications

Purification and Characterization of Novel Whey Glycoprotein WGP-88 Which Binds to a Monoclonal Antibody to PAS-4 Glycoprotein in the Bovine Milk Fat Globule Membrane

Purification and Characterization of Novel Whey Glycoprotein WGP-88 Which Binds to a Monoclonal Antibody to PAS-4 Glycoprotein in the Bovine Milk Fat Globule Membrane

Patients with anaemia can shift from kidney to liver production of erythropoietin as shown by glycoform analysis

Characterization of Sugar Moieties of a Cell Division Factor from Tobacco 2B-13 Cells

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