Recent Chemical Investigations of Bacterial Toxins

Eaton, Monroe D.

doi:10.1128/br.2.1.3-45.1938

Cited by 11 publications

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“…The diffusion constant of the toxin has been redetermined by the method of Lamm and Poison (5). EXPERIMENTAL 1. Diphtheria toxin A detailed study of the sedimentation behavior of the highly purified diphtheria toxin described in previous papers (8,9) was made in the standard Svedberg oil turbine ultracentrifuge.…”

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The Ultracentrifugal Analysis of Diphtheria Proteins.

Petermann¹,

Pappenheimer²

1941

J. Phys. Chem.

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1. Purified diphtheria toxin has a pH stability range of 5.6 to 10.1 in buffers 0.172 molar in sodium chloride.2. In buffered salt solutions at pH 7.3 to 7.5 the sedimentation rate of the toxin is independent of concentration between 0.24 and 1.02 per cent protein.3. The diffusion constant of the toxin is D10 = 6.0 X 10~7 and its molecular weight is 74,000. The ratio of major to minor axes is 4.7:1.4. The molecular weight of horse antitoxic pseudoglobulin is 184,000. The ratio of its major to minor axes is 7.0:1.5. The antitoxic protein obtained by splitting antitoxic pseudoglobulin with pepsin at pH 4.2 has a sedimentation constant of 5.7 X 10-13, a diffusion constant of 5.0 X 10-7, and a molecular weight of 113,000. The ratio of its major to minor axes is 5.3:1.6. The increase in immunological potency of the digested antitoxin is directly proportional to its decrease in size; none of the activity has been lost by this treatment.7. The agreement of the change in calculated axis ratios with the changes in size, potency, and carbohydrate content is strong evidence that an actual change in symmetry has occurred.8. The inactive pseudoglobulin associated with diphtheria antitoxin is split by pepsin in the same way as is the antitoxin.

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“…Presented at the Seventeenth Colloid Symposium, held at Ann Arbor, Michigan, June 6-8, 1940 1. This investigation was supported by a Grant-in-Aid from the Committee on Scientific Research of the American Medical Association.…”

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