Crystallization and preliminary crystallographic studies of the recombinant antitumour lectin from the edible mushroom Agrocybe aegerita
β Scribed by Na Yang; Xin Tong; Ye Xiang; Ying Zhang; Hui Sun; Da-Cheng Wang
- Book ID
- 104003439
- Publisher
- Elsevier Science
- Year
- 2005
- Tongue
- English
- Weight
- 154 KB
- Volume
- 1751
- Category
- Article
- ISSN
- 1570-9639
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β¦ Synopsis
The antitumour lectin from Agrocybe aegerita, named AAL, shows strong inhibition effects on human and mouse tumour cells via apoptosis induction activity. Recombinant AAL (rAAL) has been expressed and purified. Both rAAL and rAAL -lactose complex have been crystallized and their X-ray diffraction data were collected to resolutions of 1.9 A Λand 1.6 A Λ, respectively. Both crystals belong to space group
π SIMILAR VOLUMES
Lectins or agglutinins are proteins with affinity for specific sugar residues. Peanut agglutinin (PNA) and the lectin from the edible mushroom (Agaricus bisporus, ABL) both bind to the disaccharide galactosyl beta-1,3-N-acetyl galactosamine alpha-. This is expressed in keratinocytes as an O-linked c
The tetrameric KMΨ lectin from the seeds of Artocarpus integrifolia has, when compared to other plant lectins, the singular property of directly inducing neutrophil migration into the peritoneal cavity or into the air pouch of rats. This protein crystals have been grown and they belong to the orthor