Biomaterial Database

Circular dichroism studies on the effects of sodium dodecyl sulfate on the conformation of some phytohemagglutinins. 1978

B Jirgensons

Conformation and conformational transitions of phytohemagglutinins (lectins) from Arachis hypogaea (peanut), Lens culinaris (lentil), Glycine max (soybean), and Ricinus communis (castor bean) were studied by the circular dichroism probe. The lectins were found to possess a high amount of the pleated sheet (beta) conformation. The tertiary structure and main chain conformation of the lectins were disorganized by sodium dodecyl sulfate (SDS) and the main chain was reconstructed by relatively high concentrations of SDS (weight ratio of SDS to protein about 5-8 to 1) into new orders of higher helix content than in the native protein. More helix was formed in acid solutions than in nearly neutral solutions. The disorganization of the native tertiary structure by SDS was expressed in a decrease of the circular dichroism bands related to the tyrosine and tryptophan chromophores and in appearance of the vibronic fine structure in the phenylalanine band zone. The tertiary structure of the L. culinaris and R. communis lectins was more sensitive to SDS than the tertiary structure of the two other lectins.

UI	MeSH Term	Description	Entries
D011487	Protein Conformation	The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).	Conformation, Protein,Conformations, Protein,Protein Conformations
D002942	Circular Dichroism	A change from planar to elliptic polarization when an initially plane-polarized light wave traverses an optically active medium. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)	Circular Dichroism, Vibrational,Dichroism, Circular,Vibrational Circular Dichroism
D012276	Ricin	A protein phytotoxin from the seeds of Ricinus communis, the castor oil plant. It agglutinates cells, is proteolytic, and causes lethal inflammation and hemorrhage if taken internally.	Castor Bean Lectin,Lectin, Castor Bean,Lectin, Ricinus,Ricin Toxin,RCA 60,RCA60,Ricin A Chain,Ricin B Chain,Ricin D,Ricin I,Ricinus Toxin,A Chain, Ricin,B Chain, Ricin,Ricinus Lectin,Toxin, Ricin,Toxin, Ricinus
D012967	Sodium Dodecyl Sulfate	An anionic surfactant, usually a mixture of sodium alkyl sulfates, mainly the lauryl; lowers surface tension of aqueous solutions; used as fat emulsifier, wetting agent, detergent in cosmetics, pharmaceuticals and toothpastes; also as research tool in protein biochemistry.	Sodium Lauryl Sulfate,Irium,Dodecyl Sulfate, Sodium,Lauryl Sulfate, Sodium,Sulfate, Sodium Dodecyl,Sulfate, Sodium Lauryl
D013045	Species Specificity	The restriction of a characteristic behavior, anatomical structure or physical system, such as immune response; metabolic response, or gene or gene variant to the members of one species. It refers to that property which differentiates one species from another but it is also used for phylogenetic levels higher or lower than the species.	Species Specificities,Specificities, Species,Specificity, Species
D013056	Spectrophotometry, Ultraviolet	Determination of the spectra of ultraviolet absorption by specific molecules in gases or liquids, for example Cl2, SO2, NO2, CS2, ozone, mercury vapor, and various unsaturated compounds. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)	Ultraviolet Spectrophotometry
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