The presence of a folate binding protein of high-affinity type (affinity constant 5 · 109M−1, maximum folate binding 3 nM) in human amniotic fluid was demonstrated in equilibrium dialysis experiments (37°C, pH 7.4) with the radioligand3H-folate. Dissociation of3H-folate from the binding protein was slow at pH 7.4 but rapid at pH 3.5. By use of rabbit antibodies against low molecular weight folate binding protein from human milk we determined the concentration of folate binding protein in 5 amniotic fluids (range 1.5–2.3 nM) in an Enzyme-Linked Immunosorbent Assay (ELISA). ultrogel AcA 44 chromatography of amniotic fluid showed that immunoreactive and radioligand bound folate binding protein coeluted in two peaks: a major one (Mr~25 000) and a minor one (Mr~100 000).
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February 01 1990
A high-affinity folate binding protein in human amniotic fluid. Radioligand binding characteristics, immunological properties and molecular size Available to Purchase
Jan Holm;
Jan Holm
1Institute of Medical Biology, Department of Clinical Chemistry, University of Tromsø, Box 977, 9001 Tromsoe, Norway
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Steen Ingemann Hansen;
Steen Ingemann Hansen
1Institute of Medical Biology, Department of Clinical Chemistry, University of Tromsø, Box 977, 9001 Tromsoe, Norway
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Mimi Høier-Madsen
Mimi Høier-Madsen
1Institute of Medical Biology, Department of Clinical Chemistry, University of Tromsø, Box 977, 9001 Tromsoe, Norway
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Publisher: Portland Press Ltd
Received:
October 09 1989
Online ISSN: 1573-4935
Print ISSN: 0144-8463
© 1990 Plenum Publishing Corporation
1990
Biosci Rep (1990) 10 (1): 79–85.
Article history
Received:
October 09 1989
Citation
Jan Holm, Steen Ingemann Hansen, Mimi Høier-Madsen; A high-affinity folate binding protein in human amniotic fluid. Radioligand binding characteristics, immunological properties and molecular size. Biosci Rep 1 February 1990; 10 (1): 79–85. doi: https://doi.org/10.1007/BF01116855
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