title: Uptake and physiological function of vitamin B12 in a photosynthetic unicellular coccolithophorid alga, Pleurochrysis carterae.
abstract: The photosynthetic coccolithophoid alga, Pleurochrysis (Hymenomonas) carterae, could take up and accumulate exogenous vitamin B12, most of which was converted into the coenzyme forms of vitamin B12. Two vitamin B12-dependent enzyme activities (methylmalonyl-CoA mutase, 2.6+/-0.4 nmol/min/mg protein and methionine synthase, 85.1+/-38.9 pmol/min/mg protein) could be found in a cell homogenate of the vitamin B12-supplemented alga. Most of the methylmalonyl-CoA mutase activity and 19.2% of the vitamin B12 accumulated by the algal cells were recovered in the macromolecular fractions with Mr of 150 kDa, although the remaining vitamin B12 was found only in free vitamin B12 fractions.
authors.affiliation: Department of Health Science, Kochi Women's University, Japan.
authors.forename: Emi
authors.initials: E
authors.lastname: Miyamoto
authors.forename: Fumio
authors.initials: F
authors.lastname: Watanabe
authors.forename: Hiroyuki
authors.initials: H
authors.lastname: Takenaka
authors.forename: Yoshihisa
authors.initials: Y
authors.lastname: Nakano
mesh_terms: D013766:5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase / Q000378:metabolism; D003038:Cobamides / Q000378:metabolism; D056890:Eukaryota / Q000378:metabolism*; D008765:Methylmalonyl-CoA Mutase / Q000378:metabolism; D010788:Photosynthesis; D014805:Vitamin B 12 / Q000302:isolation & purification / Q000378:metabolism / Q000502:physiology*
chemical_list: D003038:Cobamides; D013766:5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase; D008765:Methylmalonyl-CoA Mutase; C000913:cobamamide; D014805:Vitamin B 12