Ky. Do et al., ALPHA-LACTALBUMIN INDUCES BOVINE-MILK BETA-1,4-GALACTOSYLTRANSFERASE TO UTILIZE UDP-GALNAC, The Journal of biological chemistry, 270(31), 1995, pp. 18447-18451
We now report that alpha-lactalbumin (alpha-LA) has a novel effect on
bovine milk UDP-Gal:GlcNAc-beta 1,4 galactosyltransferase (beta 1,41-G
T) and induces the enzyme to efficiently utilize UDP-GalNAc as a donor
. In the presence of alpha-LA the enzyme transfers GalNAc to free GlcN
Ac to produce GalNAc beta 1-4GlcNAc at a rate 55% of that compared to
the rate when UDP-Gal is the donor in the absence of alpha-LA. The sti
mulation by alpha-LA is dependent on the concentrations of alpha-LA, a
cceptor, and sugar nucleotide. Interestingly, beta 1,4-GT is unable to
transfer GalNAc to Glc with or without alpha-LA. alpha-LA also stimul
ates the transfer of GalNAc from UDP GalNAc to various chitin oligomer
s, although the degree of stimulation decreases as the acceptor size i
ncreases. Thus, bovine milk beta 1,4-GT has an inherent ability to uti
lize two different sugar nucleotides and the sugar nucleotide preferen
ce is regulatable by alpha-LA.