Purification and characterization of a lectin,BPL-3, from the marine green alga <Emphasis Type="Italic">Bryopsis plumosa</Emphasis> |
| |
Authors: | Jong Won Han Kang Sup Yoon Tatyana A Klochkova Mi-Sook Hwang Gwang Hoon Kim |
| |
Institution: | (1) Department of Biology, Kongju National University, Kongju, Chungnam, 314-701, South Korea;(2) Seaweed Research Center, National Fisheries Research and Development Institute, Mokpo, 530-131, South Korea; |
| |
Abstract: | A novel lectin was isolated and characterized from Bryopsis plumosa (Hudson) Agardh and named BPL-3. This lectin showed specificity to N-acetyl-d-galactosamine as well as N-acetyl-d-glucosamine and agglutinated human erythrocytes of all blood types, showing slight preference to the type A. SDS-PAGE and
MALDI-TOF MS data showed that BPL-3 was a monomeric protein with molecular weight of 11.5 kDa. BPL-3 was a non-glycoprotein
with pI value of ∼7.0. It was stable in high temperatures up to 70°C and exhibited optimum activity in pH 5.5–10. The N-terminal
and internal amino acid sequences of the lectin were determined by Edman degradation and enzymatic digestion, which showed
no sequence homology to any other reported proteins. The full sequence of the cDNA encoding this lectin was obtained from
PCR using cDNA library, and the degenerate primers were designed from the N-terminal amino acid sequence. The size of the
cDNA was 622 bp containing single ORF encoding the lectin precursor. This lectin showed the same sugar specificity to previously
reported lectin, Bryohealin, involved in protoplast regeneration of B. plumosa. However, the amino acid sequences of the two lectins were completely different. The homology analysis of the full cDNA sequence
of BPL-3 showed that it might belong to H lectin group, which was originally isolated from Roman snails. |
| |
Keywords: | |
本文献已被 SpringerLink 等数据库收录! |
|