Elucidation of the mechanism of intrinsic factor (IF)-mediated vitamin B(12) (B(12)) binding to ileal binding sites has been hampered by the use of crude or only partially purified preparations of IF in previous studies. We have used homogeneous human IF and hog IF isolated by affinity chromatography to study [(57)Co]B(12) binding to ileal mucosal homogenates. The following observations were made: (a) Human IF-B(12) and hog IF-B(12) were bound to human, monkey, hog, dog, rabbit, mouse, hamster, and guinea pig ileal, but not jejunal, homogenates in amounts significantly greater than free B(12) or B(12) bound to five other homogeneous B(12)-binding proteins; (b) only IF-mediated B(12) binding was localized to ileal homogenates and was inhibited by EDTA; (c) values for the association constant (K(a)) for the various ileal homogenates mentioned above and human IF-B(12) and hog IF-B(12) ranged from 0.3 x 10(9) M(-1) to 13.0 x 10(9) M(-1). Apparent differences in the K(a) for human IF-B(12) and hog IF-B(12) existed in most species; (d) the number of ileal IF-B(12) binding sites per gram (wet weight) of ileal mucosa ranged from 0.3 x 10(12) to 4.9 x 10(12). The same value was always obtained with human IF-B(12) and hog IF-B(12) for any given homogenate preparation; (c) 100-fold excesses of free B(12) or human IF and hog IF devoid of B(12) did not significantly inhibit human IF-B(12) and hog IF-B(12) binding to human and hog ileal homogenates. THESE EXPERIMENTS PERFORMED WITH HOMOGENEOUS IF INDICATE THAT: (a) gastric factors other than IF are not required for B(12) binding to ileal IF-B(12)-binding sites: (b) the mechanism of ileal IF-B(12) binding is different from that of free B(12) or of B(12) bound to non-IF-B(12)-binding proteins; (c) human IF and hog IF have different structures; (d) human IF-B(12) and hog IF-B(12) bind to the same ileal binding sites; and (c) human and hog ileal IF-B(12) binding sites bind free B(12) and human and hog IF devoid of B(12) poorly, if at all.
[1]
L. Ellenbogen,et al.
Hog intrinsic factor. I. Isolation of vitamin B12-binding fractions from hog pylorus.
,
1967,
The Journal of biological chemistry.
[2]
T. Steck,et al.
THE BINDING OF KIDNEY-BEAN PHYTOHEMAGGLUTININ BY EHRLICH ASCITES CARCINOMA.
,
1965,
Biochimica et biophysica acta.
[3]
W. Castle,et al.
IN VITRO ASSAY FOR HUMAN INTRINSIC FACTOR.
,
1963,
The Journal of clinical investigation.
[4]
W. Paranchych,et al.
Studies on the absorption by guinea pig intestine of cyanocobalamin incubated with intrinsic factor.
,
1962,
The Journal of clinical investigation.
[5]
E. W. Strauss,et al.
Some species differences in the intrinsic factor stimulation of B12 uptake by small intestine in vitro.
,
1959,
The American journal of physiology.
[6]
R. Gräsbeck.
Intrinsic factor and the other vitamin B12 transport proteins.
,
1969,
Progress in hematology.
[7]
B. Cooper,et al.
INTRINSIC FACTOR-LIKE ACTIVITY IN EXTRACTS OF GUINEA PIG INTESTINE.
,
1965,
American Journal of Physiology.
[8]
W. Castle,et al.
Sequential mechanisms in the enhanced absorption of vitamin B12 by intrinsic factor in the rat.
,
1960,
The Journal of clinical investigation.