In:
Bioscience, Biotechnology, and Biochemistry, Informa UK Limited, Vol. 78, No. 12 ( 2014-12-02), p. 2036-2044
Abstract:
Two jacalin-related lectins (JRLs) were purified by mannose-agarose and melibiose-agarose from seeds of Treculia africana. One is galactose-recognizing JRL (gJRL), named T. africana agglutinin-G (TAA-G), and another one is mannose-recognizing JRL (mJRL), TAA-M. The yields of the two lectins from the seed flour were approximately 7.0 mg/g for gJRL and 7.2 mg/g for mJRL. The primary structure of TAA-G was determined by protein sequencing of lysyl endopeptic peptides and chymotryptic peptides. The sequence identity of TAA-G to other gJRLs was around 70%. Two-residue insertion was found around the sugar-binding sites, compared with the sequences of other gJRLs. Crystallographic studies on other gJRLs have shown that the primary sugar-binding site of gJRLs can accommodate Gal, GalNAc, and GalNAc residue of T-antigen (Galβ1-3GalNAcα-). However, hemagglutination inhibition and glycan array showed that TAA-G did not recognize GalNAc itself and T-antigen. TAA-G preferred melibiose and core 3 O-glycan.
Type of Medium:
Online Resource
ISSN:
0916-8451
,
1347-6947
DOI:
10.1080/09168451.2014.948376
Language:
English
Publisher:
Informa UK Limited
Publication Date:
2014
detail.hit.zdb_id:
2110940-0
SSG:
12
Permalink