α-Lactalbumin Induces Bovine Milk β1,4-Galactosyltransferase to Utilize UDP-GalNAc (*)

We now report that α-lactalbumin (α-LA) has a novel effect on bovine milk UDP-Gal:GlcNAc-β1,4-galactosyltransferase (β1,4-GT) and induces the enzyme to efficiently utilize UDP-GalNAc as a donor. In the presence of α-LA the enzyme transfers GalNAc to free GlcNAc to produce GalNAcβ1-4GlcNAc at a rate 55% of that compared to the rate when UDP-Gal is the donor in the absence of α-LA. The stimulation by α-LA is dependent on the concentrations of α-LA, acceptor, and sugar nucleotide. Interestingly, β1,4-GT is unable to transfer GalNAc to Glc with or without α-LA. α-LA also stimulates the transfer of GalNAc from UDP-GalNAc to various chitin oligomers, although the degree of stimulation decreases as the acceptor size increases. Thus, bovine milk β1,4-GT has an inherent ability to utilize two different sugar nucleotides and the sugar nucleotide preference is regulatable by α-LA.

• Publication year

  1995

• Venue

  Journal of Biological Chemistry

• Publication date

  1995-08-04

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1074/JBC.270.31.18447PMID 7629170
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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