Purification and mass spectrometric characterization of sesbania aculeata (Dhaincha) stem lectin

Sagarika Biswas; Praveen Agrawal; Ashish Saroha; Hasi R. Das

doi:10.1007/s10930-009-9206-z

Purification and mass spectrometric characterization of sesbania aculeata (Dhaincha) stem lectin

Sagarika Biswas, Praveen Agrawal, Ashish Saroha, Hasi R. Das

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

6 Scopus citations

Abstract

A glucose specific lectin (STA) was isolated from Sesbania aculeata stem by using Sephadex G-50 affinity column chromatography. The lectin is a glycoprotein having 29 kDa subunit molecular weight. Two dimensional gel electrophoresis analysis revealed that the lectin existed in two isomeric forms with varied carbohydrate content as analyzed by high performance anion exchange chromatography-pulsed amperometric detector (HPAEC-PAD). Matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) and N-terminal sequence (LDSLSFTYNNFE) analysis of this lectin showed 95% homology with stem lectin SL-I (accession no. AJ585523) from peanut plant. The nucleotide sequence of the lectin (STA) was submitted to the gene bank (accession no. EU263636).

Original language	English (US)
Pages (from-to)	391-399
Number of pages	9
Journal	Protein Journal
Volume	28
Issue number	9-10
DOIs	https://doi.org/10.1007/s10930-009-9206-z
State	Published - Dec 2009
Externally published	Yes

Keywords

2D gel electrophoresis
HPAEC-PAD
Isoforms
MALDI-TOF
Peptide sequencing
Sesbania aculeata
Stem lectin

ASJC Scopus subject areas

Analytical Chemistry
Bioengineering
Biochemistry
Organic Chemistry

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10.1007/s10930-009-9206-z

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title = "Purification and mass spectrometric characterization of sesbania aculeata (Dhaincha) stem lectin",

abstract = "A glucose specific lectin (STA) was isolated from Sesbania aculeata stem by using Sephadex G-50 affinity column chromatography. The lectin is a glycoprotein having 29 kDa subunit molecular weight. Two dimensional gel electrophoresis analysis revealed that the lectin existed in two isomeric forms with varied carbohydrate content as analyzed by high performance anion exchange chromatography-pulsed amperometric detector (HPAEC-PAD). Matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) and N-terminal sequence (LDSLSFTYNNFE) analysis of this lectin showed 95% homology with stem lectin SL-I (accession no. AJ585523) from peanut plant. The nucleotide sequence of the lectin (STA) was submitted to the gene bank (accession no. EU263636).",

keywords = "2D gel electrophoresis, HPAEC-PAD, Isoforms, MALDI-TOF, Peptide sequencing, Sesbania aculeata, Stem lectin",

author = "Sagarika Biswas and Praveen Agrawal and Ashish Saroha and Das, {Hasi R.}",

year = "2009",

month = dec,

doi = "10.1007/s10930-009-9206-z",

language = "English (US)",

volume = "28",

pages = "391--399",

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issn = "1572-3887",

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TY - JOUR

T1 - Purification and mass spectrometric characterization of sesbania aculeata (Dhaincha) stem lectin

AU - Biswas, Sagarika

AU - Agrawal, Praveen

AU - Saroha, Ashish

AU - Das, Hasi R.

PY - 2009/12

Y1 - 2009/12

N2 - A glucose specific lectin (STA) was isolated from Sesbania aculeata stem by using Sephadex G-50 affinity column chromatography. The lectin is a glycoprotein having 29 kDa subunit molecular weight. Two dimensional gel electrophoresis analysis revealed that the lectin existed in two isomeric forms with varied carbohydrate content as analyzed by high performance anion exchange chromatography-pulsed amperometric detector (HPAEC-PAD). Matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) and N-terminal sequence (LDSLSFTYNNFE) analysis of this lectin showed 95% homology with stem lectin SL-I (accession no. AJ585523) from peanut plant. The nucleotide sequence of the lectin (STA) was submitted to the gene bank (accession no. EU263636).

AB - A glucose specific lectin (STA) was isolated from Sesbania aculeata stem by using Sephadex G-50 affinity column chromatography. The lectin is a glycoprotein having 29 kDa subunit molecular weight. Two dimensional gel electrophoresis analysis revealed that the lectin existed in two isomeric forms with varied carbohydrate content as analyzed by high performance anion exchange chromatography-pulsed amperometric detector (HPAEC-PAD). Matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) and N-terminal sequence (LDSLSFTYNNFE) analysis of this lectin showed 95% homology with stem lectin SL-I (accession no. AJ585523) from peanut plant. The nucleotide sequence of the lectin (STA) was submitted to the gene bank (accession no. EU263636).

KW - 2D gel electrophoresis

KW - HPAEC-PAD

KW - Isoforms

KW - MALDI-TOF

KW - Peptide sequencing

KW - Sesbania aculeata

KW - Stem lectin

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SN - 1572-3887

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JO - Protein Journal

JF - Protein Journal

IS - 9-10

ER -

Purification and mass spectrometric characterization of sesbania aculeata (Dhaincha) stem lectin

Abstract

Keywords

ASJC Scopus subject areas

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