| Literature DB >> 9618256 |
M H Soler1, S Stoeva, W Voelter.
Abstract
The primary structure of the B chain of mistletoe lectin I, the component of a commercially available extract from Viscum album exhibiting immunomodulatory capacity, was established based on amino acid sequence analysis of the protein and peptides derived from its enzymatic digestion. It is composed of 264 residues, including seven cysteine residues and three N-linked carbohydrate chains. The amino acid sequence of MLB shows a high homology with those from other structurally related galactoside-specific lectins such as ricin and abrin with 169 and 146 identities, respectively. These results are of crucial importance in order to understand the biological activity of ML-1.Entities:
Mesh:
Substances:
Year: 1998 PMID: 9618256 DOI: 10.1006/bbrc.1998.8670
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN: 0006-291X Impact factor: 3.575