Abstract
Isolation and characterization of the ileal receptor for intrinsic factor-cobalamin.
Highlights
From the Diuisionso/€€ematoZogy a n d Oncology, Department ofMedicine, and the Department of Biochemistry, Biophysics a n d Genetics, School ofMedicine, Univeraity of Colorado Health SciencesCenter, Denver, Colorado 80262
The receptor was eluted with 5 m~ EDTA at pH 5.0, leaving behind the hog intrinsic factor-cobalamin that remained bound to the anti-hog intrinsic factor-Sepharose
We have shown previously [8] that canine ileal mucosa has a somewhat higher number of Polyacrylamide disc gel electrophoresis with 0.1%Tri- intrinsic factor-Cbl receptors than most ostpheecries
Summary
CN-[“Co]Cbl and Na-“’”l were obtained from AmershamCorp., n”’) human, hog, and canine intrinsic factor-cobalamin = 1 to 4 but not with free cobalamin, free intrinsic factor, or R protein-cobalamin. Sepharose-4B, horse spleenferritin, Escherichia coliB-galactosidase, beef liver catalase, human IgG, and ovalbumin were obtained from Sigma Chemical Co., St. Louis, MO. BioGel P-30, 100-200 mesh, Bio-Gel A-5m, 200-400 mesh, and Enzyrnotor havebeen raised in rabbits. Canine intrinsic factor was purified from caninestomachs using a procedure similar to that employedfor the purification of human intrinsic factor [18].Antibodies to various species of intrinsic factor were raised in rabbits and covalently coupled to Sepharose-4B. A preliminary report o f this work has appeared in abstractform
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