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A saturable high affinity binding site for transcobalamin II-vitamin B12 complexes in human placental membrane preparations.
P A Friedman, … , M A Shia, J K Wallace
P A Friedman, … , M A Shia, J K Wallace
Published January 1, 1977
Citation Information: J Clin Invest. 1977;59(1):51-58. https://doi.org/10.1172/JCI108621.
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Research Article

A saturable high affinity binding site for transcobalamin II-vitamin B12 complexes in human placental membrane preparations.

Abstract

Studies were designed to evaluate the binding of binding of vitamin B12 to cell membrane preparations from human placenta. The transcobalamin II-vitamin B12 complex (TCII-B12), which has a much greater affinity for the membranes than vitamin B12 alone, binds to a single saturable binding site with an approximate Ka = 7.2 mM-1. The binding requires a divalent cation and is temperature-dependent. Free TCII can compete with TCII-B12 for the binding site but has somewhat less affinity than does TCII-B12. Rat TCII-B12 has an affinity constant that is less than one-fifth that of human TCII-B12; human TCI-B12, bovine TCII-B12, hog intrinsic factor-B12 (IF-B12), and human IF-B12 do not bind to the membranes. Pretreating the membranes with trypsin causes a marked decrease in subsequent binding; this suggests the binding site includes a relatively exposed membrane protein. These data suggest that a specific cell surface receptor for the TCII-B12 complex exists in placenta. This TCII-B12 receptor can be solubilized with Triton X-100.

Authors

P A Friedman, M A Shia, J K Wallace

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