The presence of a folate binding protein of high-affinity type (affinity constant 3.1010M−1, maximum folate binding 1.4 nM) in human semen was demonstrated in equilibrium dialysis experiments (37°C, pH 7.4) with the radioligand3H-folate. Radioligand dissociation from the binding protein was slow at pH 7.4, but rapid at pH 3.5. By use of rabbit antibodies against 25 kDa human milk folate binding protein we determined the concentration of folate binding protein in 16 speciments of human semen in an enzyme-linked immunosorbent assay. The concentration of immunoreactive folate binding protein was independent of the number of spermatozoa in individual specimens. Gel filtration showed that immunoreactive and radioligand bound folate binding protein coeluted in two peaks: a major one of 100 kDa and a minor one of 25 kDa.
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Research Article|
October 01 1991
A high-affinity folate binding protein in human semen
Jan Holm;
Jan Holm
1Department of Clinical Chemistry, Central Hospital Nykøbing Falster, Nykøbing Falster, 4800, Denmark
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Steen Ingemann Hansen;
Steen Ingemann Hansen
2Department of Clinical Chemistry, Central Hospital Hillerød, Hillerød, 3400 Denmark
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Mimi Høier-Madsen
Mimi Høier-Madsen
3Department of Autoimmune Serology, State Serum Institute, Copenhagen, 2300 S Denmark
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Publisher: Portland Press Ltd
Received:
July 01 1991
Online ISSN: 1573-4935
Print ISSN: 0144-8463
© 1991 Plenum Publishing Corporation
1991
Biosci Rep (1991) 11 (5): 237–242.
Article history
Received:
July 01 1991
Citation
Jan Holm, Steen Ingemann Hansen, Mimi Høier-Madsen; A high-affinity folate binding protein in human semen. Biosci Rep 1 October 1991; 11 (5): 237–242. doi: https://doi.org/10.1007/BF01127499
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