Conversion of an apparent 100 kDa folate binding protein from human milk,choroid plexus and semen to a 25 kDa molecular species by phosphatidylinositol-specific phospholipase C |
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| Authors: | Steen Ingemann Hansen Jan Holm |
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| Affiliation: | 1. Department of Clinical Chemistry, Central Hospital Hiller?d, DK-3400, Hiller?d, Denmark
2. Department of Clinical Chemistry, Central Hospital Nyk?bing Falster, DK-4800, Nyk?bing Falster, Denmark
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| Abstract: | Gel filtration studies in the presence of Triton X-100 showed that treatment with phosphatidylinositol-specific phospholipase C reduced the apparent molecular size of the 100 kDa folate binding protein from human milk, choroid plexus and semen to 25 kDa. Cleavage of a hydrophobic glycosly phosphatidylinositol domain (a membrane anchor) inserting the protein into Triton X-100 micelles could account for this phenomenon. |
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| Keywords: | glycosyl phosphatidylinositol membrane anchor human folate binding proteins choroid plexus milk and semen |
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