Biomaterial Database

The amino-acid sequence of the alpha subunit of the mitogenic lectin from Vicia sativa. 1981

G Gebauer, and E Schiltz, and H Rüdiger

The complete amino acid sequence of the alpha chain of the mitogenic lectin from Vicia sativa has been determined. The polypeptide was digested by trypsin and chymotrypsin. The fragments were isolated and most of them were sequenced by automatic solid-phase Edman degradation. A total sequence of 52 amino acid residues was obtained which is homologous to the alpha subunits of the lectins from Pisum sativum, Lens culinaris and Vicia faba. The central part (residues 13-32) in particular is completely conserved in all four proteins. In contrast to the three other known sequences, the V. sativa alpha subunit has an additional serine at the N terminus. The differences of the related amino acid sequences of these lectins and concanavalin A, the lectin from Canavalia ensiformis, have been compared using the relative substitution frequency found in homologous proteins by McLachlan. The degree of homology decreases in the order: V. sativa greater than P. sativum greater than V. faba greater than L. culinaris greater than C, ensiformis. Prediction of the secondary structure according to Chou and Fasman reveals that the lectin alpha chain is similar to concanavalin A in the first half of the molecule whereas the C-terminal part apparently tends to form an alpha helix.

UI	MeSH Term	Description	Entries
D008970	Molecular Weight	The sum of the weight of all the atoms in a molecule.	Molecular Weights,Weight, Molecular,Weights, Molecular
D010455	Peptides	Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are considered to be larger versions of peptides that can form into complex structures such as ENZYMES and RECEPTORS.	Peptide,Polypeptide,Polypeptides
D010940	Plant Proteins	Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which PLANT PROTEINS, DIETARY is available.	Plant Protein,Protein, Plant,Proteins, Plant
D003208	Concanavalin A	A MANNOSE/GLUCOSE binding lectin isolated from the jack bean (Canavalia ensiformis). It is a potent mitogen used to stimulate cell proliferation in lymphocytes, primarily T-lymphocyte, cultures.
D000595	Amino Acid Sequence	The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.	Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D019684	Magnoliopsida	A class of vascular plants which produce flowers and seeds. They include monocotyledons, dicotyledons, and about 80% of all known plant species.	Angiosperms,Angiosperma,Angiospermae,Arecidae,Asteridae,Caryophyllidae,Commelinidae,Dicotyledoneae,Dilleniidae,Flowering Plants,Hamamelidae,Hamamelididae,Icacinales,Liliatae,Liliidae,Liliopsida,Magnoliatae,Metteniusales,Oncothecales,Rosidae,Vahliales,Zingiberidae,Angiosperm,Flowering Plant,Icacinale,Metteniusale,Oncothecale,Plant, Flowering,Plants, Flowering,Vahliale
D037102	Lectins	Proteins that share the common characteristic of binding to carbohydrates. Some ANTIBODIES and carbohydrate-metabolizing proteins (ENZYMES) also bind to carbohydrates, however they are not considered lectins. PLANT LECTINS are carbohydrate-binding proteins that have been primarily identified by their hemagglutinating activity (HEMAGGLUTININS). However, a variety of lectins occur in animal species where they serve diverse array of functions through specific carbohydrate recognition.	Animal Lectin,Animal Lectins,Isolectins,Lectin,Isolectin,Lectin, Animal,Lectins, Animal
D037121	Plant Lectins	Protein or glycoprotein substances of plant origin that bind to sugar moieties in cell walls or membranes. Some carbohydrate-metabolizing proteins (ENZYMES) from PLANTS also bind to carbohydrates, however they are not considered lectins. Many plant lectins change the physiology of the membrane of BLOOD CELLS to cause agglutination, mitosis, or other biochemical changes. They may play a role in plant defense mechanisms.	Lectins, Plant,Phytagglutinin,Plant Agglutinin,Plant Lectin,Agglutinins, Plant,Phytagglutinins,Plant Agglutinins,Agglutinin, Plant,Lectin, Plant