Interaction of native and asialo rat sublingual glycoproteins with lectins

Albert M. Wu; Anthony Herp; Shuh Chyung Song; June H. Wu; Kenneth S.S. Chang

doi:10.1016/0024-3205(95)02164-E

Interaction of native and asialo rat sublingual glycoproteins with lectins

Albert M. Wu^*
, Anthony Herp
, Shuh Chyung Song
, June H. Wu
, Kenneth S.S. Chang

^*Corresponding author for this work

Department of Microbiology and Immunology

Inst. Molec. Cell. Biol., Chang-G.
Graduate Institute of Clinical Medicine

Research output: Contribution to journal › Journal Article › peer-review

19 Scopus citations

Abstract

The binding properties of the rat sublingual glycoprotein (RSL) and its asialo product with lectins were characterized by quantitative precipitin(QPA) and precipitin inhibition(QPIA) assays. Among twenty lectins tested for QPA, native RSL reacted well only with Artocarpus integrifolia (jacalin), but weakly or not at all with the other lectins. However, its asialo product(asialo-RSL) reacted strongly with many Ga1 and Ga1NAc specific lectins- it bound best to three of the GalNAcα1→ Ser/Thr (Tn) and/or Ga1β1→ 4G1cNAc (II) active lectins [jacalin, Wistaria floribunda and Ricinus communis agglutinins] and completely precipitated each of these three lectins. Asialo-RSL also reacted well with Abrus precatorius, Glycine max, Bauhinia purpurea alba, and Maclura pomifera agglutinins and abrin-a, but not with Arachis hypogeae and Dolichos biflorus agglutinins. The interaction between asialo-RSL and lectins were inhibited by either Ga1β1 → 4G1cNAc, p-NO₂-pheny1α-Ga1NAc or both. The mapping of the precipitation and inhibition profiles leads to the conclusion that the asialo rat sublingual glycoprotein provides important ligands for II (Ga1ββ1→ 4G1cNAcβ1→) and Tn(Ga1NAcα1 → Ser/Thr) active lectins.

Original language	English
Pages (from-to)	1841-1852
Number of pages	12
Journal	Life Sciences
Volume	57
Issue number	20
DOIs	https://doi.org/10.1016/0024-3205(95)02164-E
State	Published - 06 10 1995

Keywords

asialo-RSL
lectin binding
sublingual glycoprotein

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10.1016/0024-3205(95)02164-E

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title = "Interaction of native and asialo rat sublingual glycoproteins with lectins",

abstract = "The binding properties of the rat sublingual glycoprotein (RSL) and its asialo product with lectins were characterized by quantitative precipitin(QPA) and precipitin inhibition(QPIA) assays. Among twenty lectins tested for QPA, native RSL reacted well only with Artocarpus integrifolia (jacalin), but weakly or not at all with the other lectins. However, its asialo product(asialo-RSL) reacted strongly with many Ga1 and Ga1NAc specific lectins- it bound best to three of the GalNAcα1→ Ser/Thr (Tn) and/or Ga1β1→ 4G1cNAc (II) active lectins [jacalin, Wistaria floribunda and Ricinus communis agglutinins] and completely precipitated each of these three lectins. Asialo-RSL also reacted well with Abrus precatorius, Glycine max, Bauhinia purpurea alba, and Maclura pomifera agglutinins and abrin-a, but not with Arachis hypogeae and Dolichos biflorus agglutinins. The interaction between asialo-RSL and lectins were inhibited by either Ga1β1 → 4G1cNAc, p-NO2-pheny1α-Ga1NAc or both. The mapping of the precipitation and inhibition profiles leads to the conclusion that the asialo rat sublingual glycoprotein provides important ligands for II (Ga1ββ1→ 4G1cNAcβ1→) and Tn(Ga1NAcα1 → Ser/Thr) active lectins.",

keywords = "asialo-RSL, lectin binding, sublingual glycoprotein",

author = "\{M. Wu\}, Albert and Anthony Herp and Song, \{Shuh Chyung\} and Wu, \{June H.\} and Chang, \{Kenneth S.S.\}",

year = "1995",

month = oct,

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doi = "10.1016/0024-3205(95)02164-E",

language = "英语",

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pages = "1841--1852",

journal = "Life Sciences",

issn = "0024-3205",

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number = "20",

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TY - JOUR

T1 - Interaction of native and asialo rat sublingual glycoproteins with lectins

AU - M. Wu, Albert

AU - Herp, Anthony

AU - Song, Shuh Chyung

AU - Wu, June H.

AU - Chang, Kenneth S.S.

PY - 1995/10/6

Y1 - 1995/10/6

N2 - The binding properties of the rat sublingual glycoprotein (RSL) and its asialo product with lectins were characterized by quantitative precipitin(QPA) and precipitin inhibition(QPIA) assays. Among twenty lectins tested for QPA, native RSL reacted well only with Artocarpus integrifolia (jacalin), but weakly or not at all with the other lectins. However, its asialo product(asialo-RSL) reacted strongly with many Ga1 and Ga1NAc specific lectins- it bound best to three of the GalNAcα1→ Ser/Thr (Tn) and/or Ga1β1→ 4G1cNAc (II) active lectins [jacalin, Wistaria floribunda and Ricinus communis agglutinins] and completely precipitated each of these three lectins. Asialo-RSL also reacted well with Abrus precatorius, Glycine max, Bauhinia purpurea alba, and Maclura pomifera agglutinins and abrin-a, but not with Arachis hypogeae and Dolichos biflorus agglutinins. The interaction between asialo-RSL and lectins were inhibited by either Ga1β1 → 4G1cNAc, p-NO2-pheny1α-Ga1NAc or both. The mapping of the precipitation and inhibition profiles leads to the conclusion that the asialo rat sublingual glycoprotein provides important ligands for II (Ga1ββ1→ 4G1cNAcβ1→) and Tn(Ga1NAcα1 → Ser/Thr) active lectins.

AB - The binding properties of the rat sublingual glycoprotein (RSL) and its asialo product with lectins were characterized by quantitative precipitin(QPA) and precipitin inhibition(QPIA) assays. Among twenty lectins tested for QPA, native RSL reacted well only with Artocarpus integrifolia (jacalin), but weakly or not at all with the other lectins. However, its asialo product(asialo-RSL) reacted strongly with many Ga1 and Ga1NAc specific lectins- it bound best to three of the GalNAcα1→ Ser/Thr (Tn) and/or Ga1β1→ 4G1cNAc (II) active lectins [jacalin, Wistaria floribunda and Ricinus communis agglutinins] and completely precipitated each of these three lectins. Asialo-RSL also reacted well with Abrus precatorius, Glycine max, Bauhinia purpurea alba, and Maclura pomifera agglutinins and abrin-a, but not with Arachis hypogeae and Dolichos biflorus agglutinins. The interaction between asialo-RSL and lectins were inhibited by either Ga1β1 → 4G1cNAc, p-NO2-pheny1α-Ga1NAc or both. The mapping of the precipitation and inhibition profiles leads to the conclusion that the asialo rat sublingual glycoprotein provides important ligands for II (Ga1ββ1→ 4G1cNAcβ1→) and Tn(Ga1NAcα1 → Ser/Thr) active lectins.

KW - asialo-RSL

KW - lectin binding

KW - sublingual glycoprotein

UR - https://www.scopus.com/pages/publications/0028856459

U2 - 10.1016/0024-3205(95)02164-E

DO - 10.1016/0024-3205(95)02164-E

M3 - 文章

C2 - 7475931

AN - SCOPUS:0028856459

SN - 0024-3205

VL - 57

SP - 1841

EP - 1852

JO - Life Sciences

JF - Life Sciences

IS - 20

ER -

Interaction of native and asialo rat sublingual glycoproteins with lectins

Abstract

Keywords

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