当前位置： SCI文献检索 > APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY期刊下所有文献 > Purification, characterization, and preliminary X-ray diffraction analysis of a lactose-specific lectin from Cymbosema roseum seeds.

Purification, characterization, and preliminary X-ray diffraction analysis of a lactose-specific lectin from Cymbosema roseum seeds.

Abstract：

:The unique carbohydrate-binding property of lectins makes them invaluable tools in biomedical research. Here, we report the purification, partial primary structure, carbohydrate affinity characterization, crystallization, and preliminary X-ray diffraction analysis of a lactose-specific lectin from Cymbosema roseum seeds (CRLII). Isolation and purification of CRLII was performed by a single step using a Sepharose-4B-lactose affinity chromatography column. The carbohydrate affinity characterization was carried using assays for hemagglutination activity and inhibition. CRLII showed hemagglutinating activity toward rabbit erythrocytes. O-glycoproteins from mucine mucopolysaccharides showed the most potent inhibition capacity at a minimum concentration of 1.2 microg mL(-1). Protein sequencing by mass spectrometry was obtained by the digestion of CRLII with trypsin, Glu-C, and AspN. CRLII partial protein sequence exhibits 46% similarity with the ConA-like alpha chain precursor. Suitable protein crystals were obtained with the hanging-drop vapor-diffusion method with 8% ethylene glycol, 0.1 M Tris-HCl pH 8.5, and 11% PEG 8,000. The monoclinic crystals belong to space group P2(1) with unit cell parameters a = 49.4, b = 89.6, and c = 100.8 A.

journal_name

Appl Biochem Biotechnol

journal_title

Applied biochemistry and biotechnology

authors

Rocha BA,Moreno FB,Delatorre P,Souza EP,Marinho ES,Benevides RG,Rustiguel JK,Souza LA,Nagano CS,Debray H,Sampaio AH,de Azevedo WF Jr,Cavada BS

doi

10.1007/s12010-008-8334-9

subject

Has Abstract

pub_date

2009-03-01 00:00:00

pages

383-93

issue

3

eissn

0273-2289

issn

1559-0291

journal_volume

152

pub_type

杂志文章

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