Detection of glycosaminoglycans at the one-nanogram level by 125I-cytochrome c
| Autor: | Alfred P. Fishman, Ralph Heimer, Phyllis M. Sampson |
|---|---|
| Rok vydání: | 1985 |
| Předmět: |
Radioisotope Dilution Technique
Biophysics Cytochrome c Group Biochemistry Iodine Radioisotopes Glycosaminoglycan chemistry.chemical_compound Pigment Animals Formate Horses Molecular Biology Glycosaminoglycans Ethanol Chromatography biology Microchemistry Myocardium Cytochrome c Electrophoresis Cellulose Acetate Cell Biology Cellulose acetate Electrophoresis chemistry visual_art biology.protein visual_art.visual_art_medium Gluconic acid |
| Zdroj: | Analytical Biochemistry. 151:304-308 |
| ISSN: | 0003-2697 |
| DOI: | 10.1016/0003-2697(85)90180-0 |
| Popis: | The basic protein cytochrome c forms stable ionic complexes with all known glycosaminoglycans. When labeled with 125I, cytochrome c is capable of detecting exceptionally small quantities of glycosaminoglycans. Subsequent to electrophoresis on cellulose acetate strips using pyridine formate buffer at pH 3, followed by ethanol fixation, and treatment with 125I-cytochrome c, all the known glycosaminoglycans are detected at minimum levels of 1 ng/0.25-microliter application. The method can be used for quantification of glycosaminoglycans in other electrophoretic buffer systems also. |
| Databáze: | OpenAIRE |
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