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- W1983162829 abstract "Phospholipids were iodinated with iodide by a lactoperoxidase-catalyzed reaction in the presence of controlled amounts of H2O2 which were continuously supplied by glucose oxidase + glucose. Different molecular and ionic species of inorganic iodine present in the reaction mixture (i.e., I−, I2, I3−) were eliminated by thiosulfate reduction to I− followed by gel filtration on Sephadex LH-20 which separated I− from the phospholipids completely. Final separation and identification of individual phospholipids were done on a column of silica gel H using a single solvent mixture consisting of CHCl3:CH3OH:CH3COOH:H2O (25:15:4:2, by volume). Application of phospholipases A2 and D or transesterification provided evidence to indicate a covalent iodination of the fatty acid moiety of the lipids by the enzymatic process, which apparently is substitution but could also proceed by addition to the double bonds, when present." @default.
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- W1983162829 date "1980-01-01" @default.
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- W1983162829 title "Enzymatic radioiodination of phospholipids catalyzed by lactoperoxidase" @default.
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- W1983162829 doi "https://doi.org/10.1016/0003-2697(80)90222-5" @default.
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