Physical Evidence for the Asembly of A and B Chains of Human Placental Collagen in a Single Triple Helix
| Autor: | Hanne Bentz, Klaus Kühn, Hans Peter Bächinger, Robert W. Glanville |
|---|---|
| Rok vydání: | 1978 |
| Předmět: |
Protein Denaturation
Circular dichroism Protein Conformation Precipitation (chemistry) Stereochemistry Chemistry Circular Dichroism Placenta Chorion Biochemistry Peptide Fragments Melting curve analysis Crystallography Membrane Pregnancy In vivo Humans Molecule Female Denaturation (biochemistry) Amnion Collagen Amino Acids Triple helix |
| Zdroj: | European Journal of Biochemistry. 92:563-567 |
| ISSN: | 1432-1033 0014-2956 |
| DOI: | 10.1111/j.1432-1033.1978.tb12778.x |
| Popis: | Native collagen molecules containing A and B chains were isolated from pepsin-solubilised human chorionic and amniotic membrane extracts by fractional salt precipitation and DEAE-cellulose chromatography. They exhibited a circular dichroism spectrum, and a melting curve, characteristic for a triple-helical structure. Electron microscopical investigations of their segment-long-spacing crystallites revealed a molecule similar to those of the interstitial types I, II and III collagens. After denaturation, the A and B chains were separated by DEAE-cellulose chromatography and were consistently recovered in a ratio of 1:2. Renaturation experiments indicated that only the B chains are able to reform triple-helical molecules which are stable under conditions in vivo. The data support a molecular formula A(B)2 for the native collagen molecule. |
| Databáze: | OpenAIRE |
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