A high-affinity folate binding protein in normal human leukocytes: Ligand binding characteristics,ionic charge and molecular size |
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Authors: | Jan Holm Steen Ingemann Hansen Jørgen Lyngbye |
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Affiliation: | (1) Department of Clinical Chemistry, Central Hospital Nykøbing Falster, 4800 Nykøbing Falster, Denmark;(2) Department of Clinical Chemistry, Central Hospital Hillerød, 3400 Hillerød, Denmark |
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Abstract: | ![]() High-affinity binding of [3H]folate to supernatant from homogenized human leukocytes containing large amounts of binding protein displayed apparent positive cooperativity. The DEAE-Sepharose® CL-6B chromatographic profile of the supernatant at pH 6.3 contained a major peak of folate binding (Mr approx. 25 000) in the front effluent and a smaller more acidic peak (Mr approx. 25 000) that emerged after a rise in NaCl from 30 mmol/l to 1 mol/l. Triton X-100 solubilized ceil sediment from the leukocyte homogenate contained some high-affinity folate binding activity (Mr approx 25 000), typically 5–10% of the total binding activity. |
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