Evidence for a Folic Acid Binding Protein in Human Cell Membrane

1981 ◽  
Vol 66 (3) ◽  
pp. 202-209 ◽  
Author(s):  
R. Corrocher ◽  
M.L. Pachor ◽  
L.M. Bambara ◽  
G. De Sandre
1976 ◽  
Vol 29 (1) ◽  
pp. 60-62 ◽  
Author(s):  
D W Gorst ◽  
M Courtis ◽  
I W Delamore

Blood ◽  
1973 ◽  
Vol 42 (2) ◽  
pp. 281-290 ◽  
Author(s):  
Samuel Waxman ◽  
Carol Schreiber

Abstract A radioassay for the measurement of serum folate levels using commercially available beta lactoglobulin, as the folate-binding protein, and 3H-pteroylglutamic acid (3H-PGA) is reported. The assay was run in a one-step simultaneous addition at room temperature. A standard curve was constructed to a sensitivity of 0.25-10 ng of N-methyltetrahydrofolic acid (methyl-THFA). There was a clear correlation with separation into normal (greater than 6 ng/ml), indeterminate range (3-6 ng/ml), and deficient (0-3 ng/ml), as measured by radioassay. Serums from patients receiving antibiotics had normal folate levels with this assay. 3H-PGA was also used to measure serum folic acid-binding protein (FABP). In normal serums, the mean FABP was 18 pg bound/0.4 ml serum, while in folate-deficient serums it was 133 pg bound/0.4 ml of serum. Folate-deficient patients had a fall in serum FABP to the normal range when treated with folic acid. Serum FABP, in a patient on a folate-deficient diet, increased with early folate deficiency and abruptly fell to normal with a regular diet. FABP in lysates of folate-deficient bone marrow was higher than normal marrow. Patients with B12 deficiency, multiple myeloma, cirrhosis, pregnancy, or taking oral contraceptives had normal FABP. Elevated FABP was found in two out of ten patients taking Dilantin. This radioassay and the measurement of FABP should simplify the diagnosis of folate deficiency.


10.1038/13861 ◽  
1999 ◽  
Vol 23 (2) ◽  
pp. 228-232 ◽  
Author(s):  
Jorge A. Piedrahita ◽  
Betty Oetama ◽  
Gregory D. Bennett ◽  
Janée van Waes ◽  
Barton A. Kamen ◽  
...  

1978 ◽  
Vol 60 (6) ◽  
pp. 341-349 ◽  
Author(s):  
R. Corrocher ◽  
M.L. Pachor ◽  
L.M. Bambara ◽  
A. Ambrosetti ◽  
G. DeSandre

1977 ◽  
Vol 57 (3) ◽  
pp. 156-161 ◽  
Author(s):  
D.W. Gorst ◽  
Mary Courtis ◽  
I.W. Delamore

Blood ◽  
1973 ◽  
Vol 42 (2) ◽  
pp. 291-301 ◽  
Author(s):  
Samuel Waxman ◽  
Carol Schreiber

Abstract Folate-deficient serum contains a specific folic acid-binding protein (FABP) that has a rapid association and slow dissociation rate for the binding of 3H-pteroylglutamic acid (3H-PGA). FABP is also present in normal serum but in lesser amounts. The molecular weight of FABP is less than 100,000 and may represent more than one protein. FABP elutes as a beta globulin and is recovered in the transferrin band region in polyacrylamide gel electrophoresis. FABP binds oxidized folyl-, mono-, and polyglutamates in preference to reduced folates. FABP retards the delivery and uptake of 3H-PGA into HeLa cell monolayer cultures. The characteristics of FABP suggest it to be a membrane-derived intracellular folate storage protein and perhaps an important regulator of folate uptake into the cell and a storage site for folyl polyglutamates. The characteristics of serum FABP suggest it to be similar to beta lactoglobulin (the folate-binding protein isolated from cow’s milk).


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