A receptor for formaldehyde-treated serum-albumin on human placental brush-border membrane
Takami, M; Kasuya, I; Mizumoto, K; Tsunoo, H
HERO ID
1578954
Reference Type
Journal Article
Year
1988
Language
English
PMID
| HERO ID | 1578954 |
|---|---|
| In Press | No |
| Year | 1988 |
| Title | A receptor for formaldehyde-treated serum-albumin on human placental brush-border membrane |
| Authors | Takami, M; Kasuya, I; Mizumoto, K; Tsunoo, H |
| Journal | Biochimica et Biophysica Acta |
| Volume | 945 |
| Issue | 2 |
| Page Numbers | 291-297 |
| Abstract | Formaldehyde-treated serum albumin (f-Alb) is known to be taken up and degraded by sinusoidal liver cells via receptor-mediated endocytosis. We report that125I-labeled f-Alb (125I-f-Alb) binding to human placental brush-border membranes also occurs. This binding reached equilibrium within 40 min at 37°C. Kinetic studies demonstrated the presence of saturable binding with an apparent Kd of 2.1 μg of f-Alb/ml and 0 maximal binding of 2.3 μg/mg of membrane protein at pH 7.5. Maximal binding was observed at between pH 7.5 and 8.0.125I-f-Alb binding to the membranes was little inhibited by a 1000-fold molar excess of ovalbumin, human apo-transferrin and native bovine serum albumin. No binding was observed with membranes which had been pretreated with proteinase or trypsin. This f-Alb receptor was extremely heat-stable, since the binding was not abolished even by pretreatment of the membranes at 78°C for 30 min. EDTA, Ca2+ and Mg2+ had no effect on125I-f-Alb binding, so the binding was independent of divalent cations. These data suggest that a receptor specific for f-Alb exists on human placental brush-border membranes of syncytial trophoblasts. |
| Doi | 10.1016/0005-2736(88)90491-9 |
| Pmid | 2847791 |
| Wosid | WOS:A1988R329900019 |
| Is Certified Translation | No |
| Dupe Override | No |
| Is Public | Yes |
| Language Text | English |
| Keyword | Formaldehyde treated albumin, Brush-border membrane, Receptor binding(Human placenta) |