ウシ初乳中の水溶性UDP-Gal : Gal(β1-4) Glc (or GlcNAc) (α1-3)ガラクトシルトランスフェラーゼの証明

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  • Identification of a soluble UDP-Gal: Gal (.BETA.1-4)Glc (or GlcNAc) (.ALPHA.1-3) galactosyltransferase of bovine colostrum.
  • ウシ初乳中の水溶性UDP-Gal:Gal(β1-4)Glc(or GlcNAc)(α1-3)ガラクトシルトランスフェラーゼの証明〔英文〕
  • ウシ ショニュウチュウ ノ スイヨウセイ UDP Gal Gal ベータ 1-

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A soluble UDP-Gal: Gal (α1-3) galactosyltransferase was first detected in bovine colostrum and this enzyme activity was simply assayed by using ρ-nitrophenyl-β-lactoside (Gal(β1-4)Glc-C6H5NO2, ρNP-lactoside) as an acceptor. Treating the radioactive product with α- or β-galactosidase, the radioactivity (>95%) was released by only α-galactosidase and was identified as [3H] galactose. This shows that galactosyl residue was α-linked to ρ-nitrophenyl-β-lactoside. Methylation, hydrolysis, thin layer chromatography and fluorography of the reaction product (Gal(α1-)-[3H]Gal(β1-4)Glc-ρNP) yielded 2, 4, 6-tri-O-methyl[3H]galactose, indicating that galactosyl residue had been transferred to the carbon-3 position of the terminal nonreducing β-galactosyl residue in ρ-nitrophenyl-β-lactoside. These results confirmed that the structure of the reaction product was Gal(α1-3)Gal(β-4)Glc-ρNP. The enzyme requires Mn2+ for its activity, and shows pH optimum from 6.5 to 7.5. ρ-Nitrophenyl-β-lactoside and asialo α1-acid glycoprotein were more effective as an acceptor than N-acetyllactosamine. The bovine colostrum (α1-3) galactosyltransferase could not convert human O red cells into B active cells, indicating that this enzyme preparation did not contain the activity to synthesyze human blood group B erythrocytes.

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