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  • Navigating the B(12) road: assimilation, delivery, and disorders of cobalamin.

Navigating the B(12) road: assimilation, delivery, and disorders of cobalamin.

The Journal of biological chemistry (2013-03-30)
Carmen Gherasim, Michael Lofgren, Ruma Banerjee
ABSTRACT

The reactivity of the cobalt-carbon bond in cobalamins is the key to their chemical versatility, supporting both methyl transfer and isomerization reactions. During evolution of higher eukaryotes that utilize vitamin B12, the high reactivity of the cofactor coupled with its low abundance pressured development of an efficient system for uptake, assimilation, and delivery of the cofactor to client B12-dependent enzymes. Although most proteins suspected to be involved in B12 trafficking were discovered by 2009, the recent identification of a new protein reveals that the quest for elucidating the intracellular B12 highway is still far from complete. Herein, we review the biochemistry of cobalamin trafficking.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Vitamin B12, Vetec, reagent grade, ≥98%
Sigma-Aldrich
Cobalt, powder, <150 μm, ≥99.9% trace metals basis
Sigma-Aldrich
Cobalt, granular, 99.99% trace metals basis
Sigma-Aldrich
Cobalt, powder, 2 μm particle size, 99.8% trace metals basis
Sigma-Aldrich
Cobalt, pieces, 99.5% trace metals basis
Sigma-Aldrich
Vitamin B12, BioReagent, suitable for cell culture, suitable for insect cell culture, suitable for plant cell culture, ≥98%
Sigma-Aldrich
Vitamin B12, ≥98%
Sigma-Aldrich
Cyanocobalamin, tested according to Ph. Eur.
Sigma-Aldrich
Cyanocobalamin, meets USP testing specifications
Supelco
Cyanocobalamin (B12), analytical standard
Supelco
Cyanocobalamin, pharmaceutical secondary standard, certified reference material