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Biomedical subjects

C E DOLMAN

Publications and source records attributed to C E DOLMAN.

At least 19 recordsLinked to original sources

MECHANISM OF TRYPTIC ACTIVATION OF CLOSTRIDIUM BOTULINUM TYPE E TOXIN.

Gerwing, Julia (University of British Columbia, Vancouver, B.C., Canada), Claude E. Dolman, and Arthur Ko. Mechanism of tryptic activation of Clostridium botulinum type E toxin. J. Bacteriol. 89:1176-1179. 1965.-The toxic peptide of trypsin activated Clostridium botulinum type E toxin was purified by chromatography through columns packed with Sephadex G-75 and G-50. The molecular weight of the active peptide was estimated to lie between 10,000 and 12,000. Amino acid analyses indicated that the active peptide had lost at least 18 of the amino acid residues present in the original protein. The active peptide and the original protein were found to have different N-terminal amino acid residues. The mechanism of tryptic activation apparently involves chiefly the removal of amino acids from the N-terminus of the toxin molecule.

Amino Acids↗

ISOLATION AND CHARACTERIZATION OF A TOXIC MOIETY OF LOW MOLECULAR WEIGHT FROM CLOSTRIDIUM BOTULINUM TYPE A.

Gerwing, Julia (The University of British Columbia, Vancouver, B.C., Canada), Claude E. Dolman, and Hardial S. Bains. Isolation and characterization of a toxic moiety of low molecular weight from Clostridium botulinum type A. J. Bacteriol. 89:1383-1386. 1965.-A toxic moiety of low molecular weight has been isolated from a type A strain of Clostridium botulinum, by a method involving ammonium sulfate precipitation and elution through diethylaminoethyl cellulose at pH 5.6. By means of electrophoresis and ultracentrifugation, the toxic substance was shown to be homogeneous; a molecular weight of 12,200 was calculated.

Ammonium Compounds↗

PURIFICATION AND MOLECULAR WEIGHT DETERMINATION OF CLOSTRIDIUM BOTULINUM TYPE E TOXIN.

Gerwing, Julia (The University of British Columbia, Vancouver, British Columbia, Canada), Claude E. Dolman, M. E. Reichmann, and Hardial S. Bains. Purification and molecular weight determination of Clostridium botulinum type E toxin. J. Bacteriol. 88:216-219. 1964.-A method was developed whereby type E botulinus toxin can be obtained in a highly purified state by elution through acidified diethylaminoethyl-cellulose columns. The material thus isolated appears to be electrophoretically and ultracentrifugally homogeneous. A molecular weight of 18,600 was calculated for the toxin.

Antitoxins↗

BOTULISM.

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Animals↗

Activation phenomenon of Clostridium botulinum type E toxin.

Gerwing, Julia (The University of British Columbia, Vancouver, Canada), Claude E. Dolman, and David A. Arnott. Activation phenomenon of Clostridium botulinum type E toxin. J. Bacteriol. 84:302-306. 1962-Highly purified preparations of both nonactivated and trypsin-activated type E botulinus toxins have been analyzed in an ultracentrifuge. Untreated botulinus type E toxin was found to have a sedimentation constant (S(20,w)) of 5.6 Svedberg units, whereas trypsin-activated toxins would not form a boundary under identical conditions. These and other considerations indicate that the mechanism of tryptic activation involves a fragmentation process whereby more toxic sites become exposed.

Antitoxins↗

Human botulism.

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Botulism↗