[90] α-Mannosidase, β-N-acetylhexosaminidase, and β-galactosidase from jack bean meal

Li, Yu-Teh; Li, Su-Chen

doi:10.1016/0076-6879(72)28094-6

Cited by 418 publications

(103 citation statements)

References 17 publications

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“…8-Mannosidase from Achatina fulica was a gift of Seikagaku Kogyo Co. (Tokyo, Japan). The following enzymes were purified by modifications of the published procedures; Aspergillus saitoi a(1+2)-mannosidase [24], a-mannosidase and P-N-acetylhexosaminidase from Canavalia ensiformis (jack bean) [25] and a-fucosidase and P-xylosidase from Charonia lampas [26,271. P-Xylosidase from almonds was purified from almond P-glucosidase (Sigma) by gel filtration and cation-exchange chromatography (Ashford, D., Dwek, R. A. and Rademacher, T. W., unpublished data).…”

mentioning

confidence: 99%

The beta1 2-d-xylose and alpha1 3-l-fucose substituted N-linked oligosaccharides from Erythrina cristagalli lectin. Isolation, characterisation and comparison with other legume lectins

et al. 1987

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The carbohydrate moieties of Erythrina cristagalli lectin were released as oligosaccharides by hydrazinolysis, followed by N-acetylation and reduction with NaB3H4. Fractionation of the tritium-labelled oligosaccharide mixture by Bio-Gel P-4 column chromatography and high-voltage borate electrophoresis revealed that it is composed of five neutral oligosaccharides. Structural studies by sequential exoglycosidase digestion in combination with methylation analysis and two-dimensional 'H-NMR showed that the major component was the fucosecontaining heptasaccharide Mancr3(Mancr6)(Xylfl2)Manfl4GlcNAcfl4(Fucc3)GlcNAcol. This is the first report of such a structure in plant lectins. Small amounts of the corresponding afucosyl hexasaccharide were also identified, as well as three other minor components.The structure of the heptasaccharide shows the twin characteristics of a newly established family of N-linked glycans, found to date only in plants. The characteristics are substitution of the common pentasaccharide core [Mana3(Mana6)Manfl4GlcNAcfl4GlcNAc] by (1) a D-xylose residue linked 61 -2 to the P-mannosyl residue and (2) an L-fucose residue linked a 1 4 3 to the reducing terminal N-acetylglucosamine residue.The oligosaccharide heterogeneity pattern for Erythrina cristagalli lectin was also found for the lectins from four other Erythrina species and the lectins of two other legumes, Sophora japonica and Lonchocarpus capassa.All species of the genus Erythrina tested contain Nacetyllactosamine-specific lectins that are remarkably similar in their properties [l, 21. These molecules are all glycoproteins (3 -10% neutral carbohydrate by weight) with M , approximately 60000 and are composed of two identical or nearly identical subunits. Their amino acid composition is very similar and a high degree of homology exists in the N-terminal sequences. [20] and more recently for sycamore cell culture laccase [21] and Caesalpinia pulcherrimu protease inhibitor [22].The simultaneous presence of xylose and fucose therefore appears to be a common feature of many plant glycoproteins. This combination has only been described in glycoproteins of animal origin for Helix pomatiu a-haemocyanin [23].In this paper we describe the isolation of the asparaginelinked oligosaccharides of E. cristagalli lectin, their separation by high-resolution gel permeation chromatography and highvoltage electrophoresis and their characterisation by a combination of methylation analysis, nuclear magnetic resonance and sequential exoglycosidase digestion. We also compare the oligosaccharides of E. cristagalli lectin with those of the lectins from four other species of Erythrina (E. corallodendron, E. caffra, E. latissima and E. lysistemon) and the unrelated legumes Lonchocarpus capassa and Sophora japonica.

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confidence: 99%

The beta1 2-d-xylose and alpha1 3-l-fucose substituted N-linked oligosaccharides from Erythrina cristagalli lectin. Isolation, characterisation and comparison with other legume lectins

et al. 1987

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“…lb and 1 Li & Li (1972). Vibrio cholerae neuraminidase was from Calbiochem and Pronase from Sigma Chemical Co. A standard glycopeptide product (see Fig.…”

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confidence: 99%

Hybrid sialylated N-glycans are minor constituents of normal BHK-cell glycoproteins and a prominent feature in glycoproteins of some ricin-resistant cell lines

Hughes¹,

Mills²

1985

Biochemical Journal

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Baby-hamster kidney (BHK) cells were labelled metabolically by growth in media containing radioactive sugars and the asparagine-linked glycopeptides (N-glycans) obtained by Pronase digestion of disrupted cells were fractionated by chromatography on concanavalin A-Sepharose. About 2-3% of the total [3H]galactose-or[3H]fucose-labelled glycopeptides were found to be bound tightly to the lectin column and were eluted with 500mM-methyl a-mannoside. Further analysis of these minor components by chromatography on Bio-Gel P4, lentil-lectin-Sepharose and DEAESephacel and sensitivity to a-mannosidase indicates the presence in BHK-cell glycopeptides of hybrid structures of the following form:(Fucal -.6)o_-Similar structures were identified as major features of the glycoproteins of ricinresistant mutants RicR 17 and RicR 19 as described previously for RicR21 cells [Hughes, Mills & Stojanovic (1983) Carbohydr. Res. 120, 215-234]. The RicR15 cell line also produces significant amounts of hybrid N-glycans. The studies show that the novel N-glycans accumulating in ricin-resistant mutants are derived by a metabolic pathway that exists to a minor extent in normal BHK cells.In the conversion of the asparagine-linked oligosaccharides (N-glycans) of glycoproteins from the high-mannose type into complex chains, a pentamannosyl product of the initial processing reactions is acted on by N-acetylglucosaminyltransferase

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“…Assay for Other Enzymes-Exoglycosidases were assayed using MUand p-nitrophenylglycosides in 50 mM sodium acetate buffer, pH 4.0, as described previously (24). The proteolytic activity was assayed using Azocoll as a substrate (25).…”

Section: Methodsmentioning

confidence: 99%

2-Keto-3-deoxy-d-glycero-d-galacto-nononic Acid (KDN)- and N-Acetylneuraminic Acid-cleaving Sialidase (KDN-sialidase) and KDN-cleaving Hydrolase (KDNase) from the Hepatopancreas of Oyster, Crassostrea virginica

Pavlova¹,

Yuziuk²,

Nakagawa³

et al. 1999

Journal of Biological Chemistry

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KDN (2-keto-3-deoxy-D-glycero-D-galacto-nononic acid), a sialic acid analog, has been found to be widely distributed in nature. Despite the structural similarity between KDN and Neu5Ac, ␣-ketosides of KDN are refractory to conventional sialidases. We found that the hepatopancreas of the oyster, Crassostrea virginica, contains two KDN-cleaving sialidases but is devoid of conventional sialidase. The major sialidase, KDN-sialidase, effectively cleaves ␣-ketosidically linked KDN and also slowly cleaves the ␣-ketosides of Neu5Ac. The minor sialidase, KDNase, is specific for ␣-ketosides of KDN. We were able to separate these two KDN-cleaving enzymes using hydrophobic interaction and cation-exchange chromatographies. The rate of hydrolysis of 4-methylumbelliferyl-␣-KDN (MU-KDN) by KDN-sialidase is 30 times faster than that of MU-Neu5Ac in the presence of 0.2 M NaCl, whereas in the absence of NaCl this ratio is only 8. KDNase hydrolyzes MU-KDN over 500 times faster than MU-Neu5Ac and is not affected by NaCl. KDN-sialidase purified to electrophoretically homogeneous form was found to have a molecular mass of 25 kDa and an isoelectric point of 8.4. One of the three tryptic peptides derived from KDN-sialidase contains the consensus motif, SXDXGXTW, that has been found in all conventional sialidases. Kinetic analysis of the inhibition of the hydrolysis of MU-KDN and MUNeu5Ac by 2,3-dehydro-2-deoxy-KDN (KDN2-en) and 2,3-dehydro-2-deoxy-(Neu5Ac2-en) suggests that KDN-sialidase contains two separate active sites for the hydrolysis of KDN and Neu5Ac. Both KDN-sialidase and KDNase effectively hydrolyze KDN-G M3 , KDN␣233Gal ␤134Glc, KDN␣236Gal␤134Glc, KDN␣236-N-acetylgalactosaminitol, KDN␣236(KDN␣233)N-acetylgalactosaminitol, and KDN␣236(GlcNAc␤133)N-acetylgalactosaminitol. However, only KDN-sialidase also slowly hydrolyzes G M3 , Neu5Ac␣233Gal␤134Glc, and Neu5Ac␣236Gal␤134Glc. These two KDN-cleaving sialidases should be useful for studying the structure and function of KDN-containing glycoconjugates.

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[90] α-Mannosidase, β-N-acetylhexosaminidase, and β-galactosidase from jack bean meal

Cited by 418 publications

References 17 publications

The beta1 2-d-xylose and alpha1 3-l-fucose substituted N-linked oligosaccharides from Erythrina cristagalli lectin. Isolation, characterisation and comparison with other legume lectins

The beta1 2-d-xylose and alpha1 3-l-fucose substituted N-linked oligosaccharides from Erythrina cristagalli lectin. Isolation, characterisation and comparison with other legume lectins

Hybrid sialylated N-glycans are minor constituents of normal BHK-cell glycoproteins and a prominent feature in glycoproteins of some ricin-resistant cell lines

2-Keto-3-deoxy-d-glycero-d-galacto-nononic Acid (KDN)- and N-Acetylneuraminic Acid-cleaving Sialidase (KDN-sialidase) and KDN-cleaving Hydrolase (KDNase) from the Hepatopancreas of Oyster, Crassostrea virginica

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