Nature of the molecular heterogeneity of human leukocyte interferon
- 1 August 1976
- journal article
- research article
- Published by American Society for Microbiology in Journal of Virology
- Vol. 19 (2) , 425-434
- https://doi.org/10.1128/jvi.19.2.425-434.1976
Abstract
The existence of two components of human leukocyte interferon has been recently reported. In the present study, the nature of this molecular heterogeneity was explored by affinity chromatography on immobilized micro- and macroligands, ion-exchange chromatography, and molecular sieving. Chromatography on a series of alkyl-agarose adsorbents shows, for the first time, the intrinsic hydrophobicity of human leukocyte interferon. Additionally, the separation of two interferon components is achieved by use of the alkyl-agarose as well as by the omega-aminoalkyl-agarose adsorbents. Clear-cut separation of the two components was also achieved by chromatography on BSA-CH-Sepharose and on DEAE-Bio Gel A. An important feature of these separations is that they do not require the use of denaturing conditions. The molecular weights of the leukocyte interferon components, as determined on Sephadex G-75, are quite similar or identical, approximately 26,000. Thus, the molecular heterogeneity of human leukocyte interferon can be attributed, at least in part, to differences in the hydrophobicity and ionic properties of its two components.This publication has 7 references indexed in Scilit:
- Molecular structure of human fibroblast and leukocyte interferons: probe by lectin and hydrophobic chromatographyJournal of Virology, 1975
- Molecular heterogeneity of human leukocyte interferon: Two populations differing in molecular weights, requirements for renaturation, and cross-species antiviral activityVirology, 1975
- The human interferon-albumin interaction: The influence of albumin conformationVirology, 1975
- Partial Purification of Human Interferon by Affinity ChromatographyProceedings of the National Academy of Sciences, 1974
- Selective binding of human interferon to albumin immoblized on agarose.1974
- Resolution of DL-Tryptophan by Affinity Chromatography on Bovine-Serum Albumin-Agarose ColumnsProceedings of the National Academy of Sciences, 1973
- Structural requirements of the rIn·rCn complex for Induction of human interferonJournal of Molecular Biology, 1972