Journal article
Purification of Human Leukocyte Elastase and Cathepsin G by Chromatography on Immobilized Elastin
Preparative biochemistry, v 13(1)
01 May 1983
PMID: 6552675
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Abstract
Human leukocyte elastase and cathepsin G were isolated from purulent sputum by a simple procedure involving chromatography on elastin-agarose. Salt extracts of sputum were prepared, treated with DNase, and the precipitate which formed extracted and applied to a column of soluble elastin-Sepharose 4B. Contaminating protein was eluted with 50 mM Tris, 50 mM NaCl, pH 8.0 and then two column volumes of 50 mM acetate, 1.0 M NaCl, pH 5.0. The tightly bound elastase and cathepsin G together with a trypsin-like serine protease could finally be eluted with 50 mM acetate, 1.0 M NaCl, 20% DMSO, pH 5.0. Resolution of the proteases was accomplished by cation-exchange chromatography. Disc gel electrophoresis established the purity of elastase and cathepsin G and confirmed the existence of several isozymes for each.
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Details
- Title
- Purification of Human Leukocyte Elastase and Cathepsin G by Chromatography on Immobilized Elastin
- Creators
- B. R. Viscarello - Department of Biomedical Research, Pulmonary Pharmacology Section , Stuart Pharmaceuticals, Division of ICI Americas , Wilmington, DE, 19897R. L. Stein - Department of Biomedical Research, Pulmonary Pharmacology Section , Stuart Pharmaceuticals, Division of ICI Americas , Wilmington, DE, 19897E. J. Kusner - Department of Biomedical Research, Pulmonary Pharmacology Section , Stuart Pharmaceuticals, Division of ICI Americas , Wilmington, DE, 19897D. Holsclaw - Department of Biomedical Research, Pulmonary Pharmacology Section , Stuart Pharmaceuticals, Division of ICI Americas , Wilmington, DE, 19897; Department of Pediatric Medicine , Hahnemann Medical School and Hospital , Philadelphia, PA, 19101R. D. Krell - Department of Biomedical Research, Pulmonary Pharmacology Section , Stuart Pharmaceuticals, Division of ICI Americas , Wilmington, DE, 19897
- Publication Details
- Preparative biochemistry, v 13(1)
- Publisher
- Taylor & Francis Group
- Resource Type
- Journal article
- Language
- English
- Web of Science ID
- WOS:A1983QM68700005
- Scopus ID
- 2-s2.0-0020568776
- Other Identifier
- 991019353718004721
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- Web of Science research areas
- Biochemistry & Molecular Biology