Biomaterial Database

Amino groups in Clostridium perfringens epsilon prototoxin and epsilon toxin. 1986

J Sakurai, and M Nagahama

Department of Microbiology, Faculty of Pharmaceutical Sciences, Tokushima Bunti University, Japan.

Modification with succinic anhydride (SA) of Clostridium perfringens epsilon prototoxin or toxin resulted in a loss of activation by trypsin or lethal activity, respectively. The prototoxin was more sensitive to succinylation than the toxin. On the other hand, the succinylated prototoxin was activated and cleaved by chymotrypsin, but not by trypsin. The lethal activity of the toxin was also lost after treatment with 2,3-dimethylmaleic anhydride (DMA) or 2,4,6-trinitrobenzenesulfonic acid (TNBS). When the DMA-treated toxin treated with SA or TNBS was incubated under acidic condition, it regained lethal activity. Thus modification of amino groups (lysine residues) prevented activation of the prototoxin by trypsin, and abolished lethal activity of the toxin.

UI	MeSH Term	Description	Entries
D008239	Lysine	An essential amino acid. It is often added to animal feed.	Enisyl,L-Lysine,Lysine Acetate,Lysine Hydrochloride,Acetate, Lysine,L Lysine
D008299	Maleic Anhydrides	Used in copolymerization reactions, in the Diels-Alder(diene)synthesis, in the preparation of resins, pharmaceuticals and agricultural chemicals. It is a powerful irritant and causes burns.	2,5-Furandiones,Maleic Anhydride,2,5 Furandiones,Anhydride, Maleic,Anhydrides, Maleic
D002918	Chymotrypsin	A serine endopeptidase secreted by the pancreas as its zymogen, CHYMOTRYPSINOGEN and carried in the pancreatic juice to the duodenum where it is activated by TRYPSIN. It selectively cleaves aromatic amino acids on the carboxyl side.	Alpha-Chymotrypsin Choay,Alphacutanée,Avazyme
D003016	Clostridium perfringens	The most common etiologic agent of GAS GANGRENE. It is differentiable into several distinct types based on the distribution of twelve different toxins.	Clostridium welchii
D001427	Bacterial Toxins	Toxic substances formed in or elaborated by bacteria; they are usually proteins with high molecular weight and antigenicity; some are used as antibiotics and some to skin test for the presence of or susceptibility to certain diseases.	Bacterial Toxin,Toxins, Bacterial,Toxin, Bacterial
D013329	Structure-Activity Relationship	The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.	Relationship, Structure-Activity,Relationships, Structure-Activity,Structure Activity Relationship,Structure-Activity Relationships
D013387	Succinic Anhydrides	A subclass of anhydrides with the general structure of dihydrofurandione. They can be substituted on any carbon atom. They modify and inhibit proteins and enzymes and are used in the acylation of amino- and hydroxyl groups.	Anhydrides, Succinic
D014302	Trinitrobenzenesulfonic Acid	A reagent that is used to neutralize peptide terminal amino groups.	Picrylsulfonic Acid,Trinitrobenzene Sulfonate,2,4,6-Trinitrobenzene Sulfonate,Trinitrobenzenesulfonic Acid, Sodium Salt,Sulfonate, Trinitrobenzene
D014357	Trypsin	A serine endopeptidase that is formed from TRYPSINOGEN in the pancreas. It is converted into its active form by ENTEROPEPTIDASE in the small intestine. It catalyzes hydrolysis of the carboxyl group of either arginine or lysine. EC 3.4.21.4.	Tripcellim,Trypure,beta-Trypsin,beta Trypsin

Related Publications

J Sakurai, and M Nagahama

Enzymatic activation of Clostridium perfringens epsilon prototoxin and some biological properties of activated toxin.

December 1973, The Onderstepoort journal of veterinary research,

J Sakurai, and M Nagahama

Studies on epsilon-prototoxin of Clostridium perfringens type D. Physicochemical and chemical properties of epsilon-prototoxin.

November 1975, Biochimica et biophysica acta,

J Sakurai, and M Nagahama

Identification of a lambda toxin-negative Clostridium perfringens strain that processes and activates epsilon prototoxin intracellularly.

October 2012, Anaerobe,

J Sakurai, and M Nagahama

A comparison of Clostridium perfringens epsilon toxin-toxoid and prototoxin-toxoid in the immunization of young lambs.

July 1954, American journal of veterinary research,

J Sakurai, and M Nagahama

Differential conformational environment of tryptophan in epsilon native prototoxin and active toxin from Clostridium perfringens type D.

April 2002, Journal of biochemistry, molecular biology, and biophysics : JBMBB : the official journal of the Federation of Asian and Oceanian Biochemists and Molecular Biologists (FAOBMB),

J Sakurai, and M Nagahama

Studies on epsilon-prototoxin of Clostridium perfringens type D. I. Purification methods: evidence for multiple forms of epsilon-prototoxin.

March 1969, Archives of biochemistry and biophysics,

J Sakurai, and M Nagahama

Clostridium perfringens type D epsilon prototoxin. Some chemical, immunological and biological properties of a highly purified prototoxin.

December 1973, The Onderstepoort journal of veterinary research,

J Sakurai, and M Nagahama

Physical changes in the epsilon prototoxin molecule of Clostridium perfringens during enzymatic activation.

November 1977, Infection and immunity,

J Sakurai, and M Nagahama

Conformational studies on modified proteins and peptides. VII. Conformation of epsilon-prototoxin and epsilon-toxin from Clostridium perfringens. Conformational changes associated with toxicity.

October 1973, Biochimica et biophysica acta,