ISOLATION OF GRANULES FROM EOSINOPHIL LEUCOCYTES AND STUDY OF THEIR ENZYME CONTENT
| Autor: | Gordon T. Archer, James G. Hirsch |
|---|---|
| Rok vydání: | 1963 |
| Předmět: |
Cytoplasm
Neutrophils Immunology Granulocyte Cytoplasmic Granules Article chemistry.chemical_compound Ribonucleases medicine Animals Immunology and Allergy Centrifugation Horses Cathepsin biology Research Granule (cell biology) Albumin Blood Proteins Eosinophil Cathepsins Molecular biology Enzymes Mitochondria Rats Eosinophils medicine.anatomical_structure chemistry Biochemistry biology.protein Rabbits Lysozyme Lysosomes Oxidoreductases Peroxidase |
| Zdroj: | The Journal of Experimental Medicine |
| ISSN: | 1540-9538 0022-1007 |
| DOI: | 10.1084/jem.118.2.277 |
| Popis: | Eosinophils were separated from other types of cells in horse blood or rat peritoneal fluid by centrifugation in concentrated albumin solutions. Eosinophils did not appear to be damaged by this separation procedure. A technique was also devised for isolation of cytoplasmic granules from eosinophils, thus allowing studies on enzyme content of the granules. Granules from both horse and rat eosinophils contained a number of hydrolytic enzymes, similar in variety and in concentration to those previously found in granules of rabbit polymorphonuclear leucocytes. Eosinophil granules differed from those of the rabbit granulocyte in their high content of peroxidase and the absence of lysozyme and phagocytin. On disruption of eosinophil granules by repeated freezing and thawing in saline, cathepsin, ribonuclease, arylsulfatase and beta glucuronidase were released into solution, but phosphatases were partially and peroxidase completely bound to the insoluble granule residue. Peroxidase could be extracted from the granule residue with weak acid. Eosinophil granules thus are lysosome-like structures. |
| Databáze: | OpenAIRE |
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