[HTML][HTML] Characterization of an epithelial∼ 460-kDa protein that facilitates endocytosis of intrinsic factor-vitamin B12 and binds receptor-associated protein
H Birn, PJ Verroust, E Nexø, H Hager… - Journal of biological …, 1997 - ASBMB
By using receptor-associated protein (RAP) as an affinity target, an intrinsic factor-vitamin B
12 (IF-B 12)-binding renal epithelial protein of∼ 460 kDa was copurified together with the
transcobalamin-B 12-binding 600-kDa receptor, megalin. IF-B 12 affinity chromatography of
renal cortex membrane from rabbit and man yielded the same∼ 460-kDa protein. Binding
studies including surface plasmon resonance analyses of the protein demonstrated a
calcium-dependent and high affinity binding of IF-B 12 to a site distinct from the RAP binding …
12 (IF-B 12)-binding renal epithelial protein of∼ 460 kDa was copurified together with the
transcobalamin-B 12-binding 600-kDa receptor, megalin. IF-B 12 affinity chromatography of
renal cortex membrane from rabbit and man yielded the same∼ 460-kDa protein. Binding
studies including surface plasmon resonance analyses of the protein demonstrated a
calcium-dependent and high affinity binding of IF-B 12 to a site distinct from the RAP binding …