title: Primary structure and biological activity of snake venom lectin (APL) from Agkistrodon p. piscivorus (Eastern cottonmouth).
abstract: A lectin (APL) was purified from the venom of Agkistrodon piscivorus piscivorus (Eastern cottonmouth moccasin). APL is a disulfide-linked, homodimeric protein consisting of identical monomers of molecular weight 16,200. Native rabbit and human erythrocytes were agglutinated by APL and the activity was found to be calcium-dependent. Galactose, lactose, rhamnose and EGTA strongly inhibited the hemagglutination activity of APL. The complete amino acid sequence determined by Edman sequencing of the S-pyridylethylated derivative and its peptides derived from enzymatic digestion indicate the structure of APL to be highly homologous with lectins and the platelet glycoprotein Ib (GPIb)-binding proteins isolated from other snake venoms. These results suggest that APL belongs to the C-type beta-galactoside binding lectin family which possess structural similarities with the C-terminal carbohydrate-recognition domain (CRD) of animal membrane lectins.
authors.affiliation: Department of Microbiology, Faculty of Pharmacy, Meijo University, Nagoya, Japan. ykomori@meijo-u.ac.jp
authors.forename: Y
authors.initials: Y
authors.lastname: Komori
authors.forename: T
authors.initials: T
authors.lastname: Nikai
authors.forename: T
authors.initials: T
authors.lastname: Tohkai
authors.forename: H
authors.initials: H
authors.lastname: Sugihara
mesh_terms: D017836:Agkistrodon / Q000502:physiology*; D000595:Amino Acid Sequence; D000818:Animals; D002118:Calcium / Q000378:metabolism; D006384:Hemagglutination / Q000187:drug effects*; D006801:Humans; D037102:Lectins / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000633:toxicity*; D008969:Molecular Sequence Data; D011817:Rabbits; D016415:Sequence Alignment; D012910:Snake Venoms / Q000737:chemistry / Q000633:toxicity*
chemical_list: D037102:Lectins; D012910:Snake Venoms; D002118:Calcium