Leon E. Rosenberg (auth.), Harry Harris, Kurt Hirschhorn's Advances in Human Genetics 6 PDF

By Leon E. Rosenberg (auth.), Harry Harris, Kurt Hirschhorn (eds.)

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4) also exist in these normal human cells. 89 Since methylmalonyl-CoA mutase, the apoenzyme which requires Ado-Cbl for activity, is thought to be a mitochondrial protein, 55 whereas the methyitransferase apoenzyme appears to be cytoplasmic,168 it is obvious that complete understanding of intracellular cobalamin metabolism must also include knowledge of the subcellular transport and organellar localization of the vitamin and its coenzyme forms. 115 have proposed that cobalamin bound to TC II enters cells by a series of steps which include adsorption to membrane receptors, endocytosis of intact TC 11Cbl, formation of a secondary lysosomal vacuole in which the Cbl is split from TC II, and entry of Cbl into the mitochondrion (Fig.

The second is a dimethylbenzimidazole ribotide portion extending down from the plane of the corrin ring. 57 The molecule is completed by coordinate linkage of one of several different radicals to the cobalt atom. This radical extends up from the corrin plane. Thus cyanocobalamin (CNCbI), the commercial form of vitamin B 12 , is formed by attachment of a cyanide radical to the cobalt atom. This compound, however, is an artifact of the chemical procedures used to isolate cobalamins and does not occur naturally in bacteria or animal tissues.

Failed to oxidize 14C-propionate or 14C-methylmalonate to 14C02, thus demonstrating a block in methyl malonate metabolism and providing a convenient tissue source for additional biochemical investigation. 128 Fibroblasts from this boy contained less than 10% of normal Ado-Cbl content, suggesting a defect in Ado-Cbl synthesis from precursor vitamin. His fibroblasts, too, were B12 responsive (Fig. J ~ 6 8. DAYS OF STUDY OLI---L--~ILO---L--~2LO---L--~3LO---L--~4LO---L--~5~0---L-J 250 ~ '" 500 750 >:r ...

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