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Chemical characterization of the lectin from Amaranthus leucocarpus syn. hypocondriacus by 2-D proteome analysis.

Abstract：

:In this work, we characterized chemically the N-acetyl-D-galactosamine specific lectin from Amaranthus leucocarpus syn hypocondriacus lectin (ALL). It is a dimeric glycoprotein composed by three isoforms with pl at 4.8, 4.9, and 5.2. Circular dichroism analysis indicated that the secondary structure of ALL contains 45% of \bibeta-sheet and 5% of \bialpha-helix. Amino acid sequence of the purified lectin and its isoforms was determined from peptides obtained after trypsin digestion by MALDI-TOF (Matrix assisted laser desorption ionization-time of flight). The tryptic peptides prepared from the purified lectin and the three isoforms showed different degrees (80 to 83%) of identity with the amino acid sequence belonging to a previously described high nutritional value protein from A. hypocondriacus not shown at the time to be a lectin. Furthermore, analysis of tryptic peptides obtained from ALL previously treated with peptide N-glycosidase, revealed a 93% identity with the aforementioned protein. Presence of N-glycosidically linked glycans of the oligomannosidic type and, in minor proportion, of the N-acetyllactosaminic type glycans was determined by affinity chromatography on immobilized Con A.

journal_name

Glycoconj J

journal_title

Glycoconjugate journal

authors

Hernández P,Debray H,Jaekel H,Garfias Y,Jiménez Md Mdel C,Martínez-Cairo S,Zenteno E

doi

10.1023/a:1013760915738

subject

Has Abstract

pub_date

2001-04-01 00:00:00

pages

321-9

issue

4

eissn

0282-0080

issn

1573-4986

journal_volume

18

pub_type

杂志文章

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