The isolation and characterization of lysozyme from human foetal membranes: A comparison with the enzyme from other sources
| Autor: | John R. Walsh, Hugh D. Niall, Peter M. Barling, Marie J. John |
|---|---|
| Rok vydání: | 1985 |
| Předmět: |
Amniotic fluid
Physiology Placenta Extraembryonic Membranes Biology Biochemistry High-performance liquid chromatography chemistry.chemical_compound Egg White Pregnancy Decidua medicine Humans Amnion Amino Acids Molecular Biology Muramidase Chromatography High Pressure Liquid chemistry.chemical_classification Chromatography Milk Human Elution General Medicine Amniotic Fluid Chromatography Ion Exchange Electrophoresis Enzyme medicine.anatomical_structure chemistry Chromatography Gel Electrophoresis Polyacrylamide Gel Female Lysozyme |
| Zdroj: | Comparative Biochemistry and Physiology Part B: Comparative Biochemistry. 81:509-513 |
| ISSN: | 0305-0491 |
| Popis: | 1. 1. Lysozyme (muramidase) was isolated from an acidic extract of human foetal membranes by adsorption and elution from octadecyl silica. It was further purified by gel-filtration and ion-exchange. 2. 2. The final product was homogeneous by high performance liquid chromatography (h.p.l.c.) and electrophoresis. It was indistinguishable from human milk lysozyme by all criteria investigated, including amino acid composition, electrophoretic mobility, retention time on h.p.l.c. and sequence of the first nine residues. 3. 3. Human uterine decidual tissue was shown to contain a similar concentration of lysozyme to foetal membranes. The enzyme was also present at lower concentrations in amnion, placenta and amniotic fluid. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|