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• W1781165902 abstract "The streptomycin precursor (L) was purified and its properties were studied. The precursor L in the crude aqueous solution was first precipitated as its reineckate, and then recrystallized from hot water. The L reineckate was decomposed to L sulfate and the protonated reineckate by acidification with sulfuric acid. After removing the protonated reineckate with Amber lite X AD-2, the L sulfate solution was subjected to column chromatography on Sephadex C-25. Gradient elution was performed with aqueous ammonium acetate solution. The L-containing fractions were dried thoroughly in vacuo till no free ammonium acetate remained. The acetate form of L thus obtained was changed to sulfate form with sulfuric acid and acetone, obtaining white powder or L sulfate. The L gave the positive maltol reaction, the intensity of which was equal to that given by the same amount of streptomycin on the basis of bioassay. It was bioautographically shown that dephosphorylation of L by alkaline phosphatase or lanthanum hydroxide gave rise to formation of streptomycin. The molar concentration of the phosphorus in L was same as that of streptomycin derived from the L. These results suggested that the L was phosphorylated streptomycin; one mole phosphoric acid being attached to one mole streptomycin with ester bond. The natural precursor (called L) of streptomycin was hydrolyzed with sulfuric acid under the same conditions as that used for cleaving streptomycin into the streptidine and streptobiosamine moieties, and white needle-shaped crystal was obtained by neutralization of the hydrolyzate. This crystal was converted to streptidine by intestinal alkaline phosphatase, showing that the crystalline material is a phosphorvlated streptidine. Furthermore, from the amount of periodate consumed by this crystalline material, it was considered that the hydroxyl group on C-6 of the streptidine moiety was phosphorylated. The mother liquid of the above hydrolyzate gave the same electrophoretical pattern as that given by the corresponding portion of hydrolyzate of streptomycin. From these results, L was considered to be a phosphorylated streptomycin, in which the hydroxyl group on C-6 of the streptidine moiety was phosphorylated." @default.
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• W1781165902 date "1969-10-01" @default.
• W1781165902 modified "2023-10-16" @default.
• W1781165902 title "Biosynthesis of Streptomycin" @default.
• W1781165902 doi "https://doi.org/10.1080/00021369.1969.10859493" @default.
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