You are here:
| Reference : Biosynthesis of type IV and V (alpha A-alpha B) collagens by human placenta. |
| Scientific journals : Article | |||
| Human health sciences : Reproductive medicine (gynecology, andrology, obstetrics) | |||
| http://hdl.handle.net/2268/84488 | |||
| Biosynthesis of type IV and V (alpha A-alpha B) collagens by human placenta. | |
| English | |
Foidart, Jean-Michel  [Université de Liège - ULg > Département des sciences cliniques > Gynécologie - Obstétrique - Labo de biologie des tumeurs et du développement >] | |
| Tryggvason, K. [ > > ] | |
| Robey, P. G. [ > > ] | |
| Liotta, A. [ > > ] | |
| Martin, G. R. [ > > ] | |
| 1981 | |
| Collagen and Related Research | |
| Gustav Fischer Verlag | |
| 1 | |
| 2 | |
| 137-50 | |
| International | |
| 0174-173X | |
| Stuttgart | |
| Germany | |
| [en] The collagenous proteins synthesized by placenta in organ culture were characterized. Types I and III collagen accounted for about two-thirds of the collagenous protein produced by the tissue while type IV procollagen comprised around 10%. Type IV collagen contained two chains of 185,000 and 175,000 daltons which are genetically distinct from one another as determined by a peptide mapping procedure. The type IV procollagen was identical to that produced by other tissues based on ratios of 3- to 4-hydroxyproline and hydroxyproline to proline, and on the pattern produced upon polyacrylamide gel electrophoresis before and after peptide mapping procedures. About 20% of the collagen resembled type V collagen in the proportions of 3- and 4-hydroxyproline to proline and of hydroxylysine to lysine, in solubility, and in peptide maps. However, it contained disulfide linked chains larger than those found in the type V collagen solubilized by pepsin. Following pepsin treatment, the disulfide bonds were removed and the mobility of the chains of the labeled protein resembled those in type V collagen. It is likely that the disulfide linked protein represents the intact type V collagen molecule. | |
| http://hdl.handle.net/2268/84488 |
There is no file associated with this reference.
All documents in ORBi are protected by a user license.
