The mechanism of cobalamin binding to hog intrinsic factor

Eric L. Lien, Leon Ellenbogen, P. Y. Law, J. M. Wood

Research output: Contribution to journalArticlepeer-review

14 Scopus citations


Circular dichroism studies on the methylcobalamin-intrinsic factor complex, together with studies on the carbethoxylation of histidine residues in this complex, indicate that 5,6 dimethylbenzimidazole is probably displaced by a histidine residue of intrinsic factor which coordinates to the cobalt atom at the sixth coordination site. In addition, the stability of the CoC σ bond for methylcobalamin bound to intrinsic factor is identical to that stability measured for the free methyl-cobinamide-histidine complex, but considerably different from the stability of this σ bond in free methylcobalamin.

Original languageEnglish (US)
Pages (from-to)730-735
Number of pages6
JournalBiochemical and Biophysical Research Communications
Issue number3
StatePublished - Dec 10 1973


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