Purification and partial characterization of a lectin from Canavalia grandiflora Benth. seeds

被引：21
|
作者：
Ceccatto, VM
Cavada, BS
Nunes, EP
Nogueira, NAP
Grangeiro, MB
Moreno, FBMB
Teixeira, EH
Sampaio, AH
Alves, MAO
Ramos, MV
Calvete, JJ
Grangeiro, TB
机构：
[1] Univ Estadual Ceara, Dept Geociencias, BR-60451970 Fortaleza, Ceara, Brazil
[2] Univ Fed Ceara, BioMol Lab, BR-60451970 Fortaleza, Ceara, Brazil
[3] Univ Fed Ceara, Dept Biol, BR-60451970 Fortaleza, Ceara, Brazil
[4] Univ Fed Ceara, Lab Bioquim Marinha, BR-60451970 Fortaleza, Ceara, Brazil
[5] Inst Biomed, Valencia, Spain
来源：
PROTEIN AND PEPTIDE LETTERS | 2002年 / 9卷 / 01期
关键词：
D O I：
10.2174/0929866023409002
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
A D-glucose/D-mannose specific lectin from seeds of Canavalia grandiflora (ConGF) was purified by affinity chromatography on Sephadex G-50. By SDS-PAGE ConGF yielded three protein bands with apparent molecular masses of 29-30 kDa (alpha chain), 16-18 kDa (beta fragment) and 12-13 kDa (gamma fragment), like other related lectins from the genus Canavalia (Leguminosae). ConGF strongly agglutinates rabbit erythrocytes, has a high content of ASP and SER, and its N-terminal sequence (30 residues) is highly similar to the sequences of other related lectins from subtribe Diocleinae.
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收藏
页码：67 / 73
页数：7
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