Human Lymphotoxin: Purification and Some Properties

Lymphotoxin is secreted by human lymphocytes stimulated with phytohemagglutinin in vitro. Combinations of DEAE-cellulose and Sephadex chromatography, acrylamide gel electrophoresis, and isoelectric focusing were used to purify lymphotoxin 2000- to 4000-fold; 15-25% of the activity has been recovered...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1973-01, Vol.70 (1), p.27-30
Main Authors: Granger, G. A., Laserna, E. C., Kolb, W. P., Chapman, F.
Format: Article
Language:English
Subjects:
Albumins
Biological Sciences: Immunology
Cells, Cultured
Centrifugation
Centrifugation, Density Gradient
Chromatography, DEAE-Cellulose
Chromatography, Gel
Culture Media
Dialysis
Electrophoresis
Electrophoresis, Polyacrylamide Gel
Elution
Gels
Hemoglobins
Humans
Isoelectric Focusing
Lectins - pharmacology
Lymphocytes
Lymphocytes - analysis
Lymphocytes - drug effects
Molecular weight
Molecules
Toxins, Biological - isolation & purification
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Summary:Lymphotoxin is secreted by human lymphocytes stimulated with phytohemagglutinin in vitro. Combinations of DEAE-cellulose and Sephadex chromatography, acrylamide gel electrophoresis, and isoelectric focusing were used to purify lymphotoxin 2000- to 4000-fold; 15-25% of the activity has been recovered. Lymphotoxin appears to be a weakly charged molecule(s) of molecular weight about 90,000-100,000 that migrates in Pevikon block electrophoresis as a β - or α2globulin. It is a discrete molecule(s), because it is completely separable from medium serum proteins and carrier and phytohemagglutinin proteins. Isoelectric-focusing studies indicate that there may be a limited heterogeneity among lymphotoxin molecules.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.70.1.27