|
Repositorio Atenea de la Facultad de Ciencias, UNAM >
Repositorio Ciencias >
FACULTAD DE CIENCIAS >
Ciencias >
Please use this identifier to cite or link to this item:
http://hdl.handle.net/11154/1440
|
Title: | Purification and characterization of a lectin from the white shrimp Litopenaeus setiferus (Crustacea decapoda) hemolymph |
Authors: | Alpuche, J Pereyra, A Agundis, C Rosas, C Pascual, C Slomianny, MC Vazquez, L Zenteno, E |
Issue Date: | 2005 |
Abstract: | A 291-kDa lectin (LsL) was purified from the hemolymph of the white shrimp Litopenaeus setiferus by affinity chromatography on glutaraldehyde-fixed stroma from rabbit erythrocytes. LsL is a heterotetramer of two 80-kDa and two 52-kDa subunits, with no covalently-liked carbohydrate, and mainly composed by aspartic and glutamic acids, glycine and alanine, with relatively lower methionine and cysteine contents. Edman degradation indicated that the NH2-terminal of the 80-kDa subunit is composed DASNAQKQHDVNFLL, whereas the NH2-terminal of the 52-kDa subunit is blocked. The peptide mass fingerprint of LsL was predicted from tryptic peptides from each subunit by MALDI-TOF, and revealed that each subunit showed 23 and 22%, respectively, homology with the hemocyanin precursor from Litopenaeus vannamei. Circular dichroism analysis revealed beta sheet and alpha helix contents of 52.7 and 6.1%, respectively. LsL agglutinate at higher titers guinea pig, murine, and rabbit erythrocytes its activity is divalent cation-dependent. N-acetylated sugars, such as GlcNAc, GaINAc, and NeuAc, were the most effective inhibitors of the LsL hemagglutinating activity. Sialylated O-glycosylated proteins, such as bovine submaxillary gland mucin, human IgA, and fetuin, showed stronger inhibitory activity than sialylated N-glycosylated proteins, such as human orosomucoid, IgG, transferrin, and lactoferrin. Desialylation of erythrocytes or inhibitory glycoproteins abolished their capacity to bind LsL, confirming the relevance of sialic acid in LsL-ligand interactions. (c) 2005 Elsevier B.V. All rights reserved. |
URI: | http://hdl.handle.net/11154/1440 |
ISSN: | 0304-4165 |
Appears in Collections: | Ciencias
|
Files in This Item:
There are no files associated with this item.
|
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.
|