DOI: 10.1085/jgp.25.3.487. PURIFIED DIPHTHERIA ANTITOXIN IN THE ULTRACENTRIFUGE AND IN THE ELECTROPHORESIS APPARATUS

PURIFIED DIPHTHERIA ANTITOXIN IN THE ULTRACENTRIFUGE AND IN THE ELECTROPHORESIS APPARATUS

10.1085/jgp.25.3.487

Crossref journal-article

Rockefeller University Press

Journal of General Physiology (291)

Abstract

Ultracentrifugation studies of diphtheria antitoxin showed that: 1. Purified antitoxin of high activity obtained from horse plasma without enzymatic treatment has exactly the same sedimentation constant as the globulin fraction obtained in a similar way from normal horse plasma s20water = 6.9 x 10–13. 2. Purified antitoxin obtained with trypsin digestion of the toxin-antitoxin complex has a sedimentation constant of s20water = 5.5 ± 0.1 x 10–13, a diffusion constant of D20water = 5.76 x 10–7, and a molecular weight of about 90,000. Electrophoresis experiments demonstrated that: 1. The trypsin-purified antitoxin has an isoelectric point not far from pH 7.0. 2. The reversible spreading noticed at about pH 7.3 cannot be attributed to heterogeneous preparation. 3. The large increase in the γ-globulin fraction occurring during immunization consists either of antitoxin of various degrees of activity or of some inert protein in addition to the antitoxin.

Bibliography

Rothen, A. (1942). PURIFIED DIPHTHERIA ANTITOXIN IN THE ULTRACENTRIFUGE AND IN THE ELECTROPHORESIS APPARATUS. Journal of General Physiology, 25(3), 487â496.

Authors 1

Alexandre Rothen (first)

References 0 Referenced 13

None

Dates

Type	When
Created	21 years, 3 months ago (May 13, 2004, 5:20 p.m.)
Deposited	4 years, 11 months ago (Oct. 3, 2020, 3 p.m.)
Indexed	1 year, 9 months ago (Nov. 24, 2023, 3:13 a.m.)
Issued	83 years, 7 months ago (Jan. 20, 1942)
Published	83 years, 7 months ago (Jan. 20, 1942)
Published Online	83 years, 7 months ago (Jan. 20, 1942)
Published Print	83 years, 7 months ago (Jan. 20, 1942)

Funders 0

None

BibTeX

@article{Rothen_1942, title={PURIFIED DIPHTHERIA ANTITOXIN IN THE ULTRACENTRIFUGE AND IN THE ELECTROPHORESIS APPARATUS}, volume={25}, ISSN={0022-1295}, url={http://dx.doi.org/10.1085/jgp.25.3.487}, DOI={10.1085/jgp.25.3.487}, number={3}, journal={Journal of General Physiology}, publisher={Rockefeller University Press}, author={Rothen, Alexandre}, year={1942}, month=jan, pages={487–496} }

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  "abstract": "<jats:p>Ultracentrifugation studies of diphtheria antitoxin showed that:</jats:p>\n               <jats:p>1. Purified antitoxin of high activity obtained from horse plasma without enzymatic treatment has exactly the same sedimentation constant as the globulin fraction obtained in a similar way from normal horse plasma s20water = 6.9 x 10\u201313.</jats:p>\n               <jats:p>2. Purified antitoxin obtained with trypsin digestion of the toxin-antitoxin complex has a sedimentation constant of s20water = 5.5 \u00b1 0.1 x 10\u201313, a diffusion constant of D20water = 5.76 x 10\u20137, and a molecular weight of about 90,000.</jats:p>\n               <jats:p>Electrophoresis experiments demonstrated that:</jats:p>\n               <jats:p>1. The trypsin-purified antitoxin has an isoelectric point not far from pH 7.0.</jats:p>\n               <jats:p>2. The reversible spreading noticed at about pH 7.3 cannot be attributed to heterogeneous preparation.</jats:p>\n               <jats:p>3. The large increase in the \u03b3-globulin fraction occurring during immunization consists either of antitoxin of various degrees of activity or of some inert protein in addition to the antitoxin.</jats:p>",
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