Glycolipid glycosyl transferases of a hamster cell line in culture. I. Kinetic constants, substrate and donor nucleotide sugar specificities.
The properties of enzymes catalysing the transfer of a galactose from UDP-galactose to exogenous ceramide monohexoside and ceramide di-hexoside derived from the Syrian hamster cell line NIL 2 were studied. The products of these enzymes were characterized by chemical and enzymatic methods. Kinetic analyses showed that the enzymes are susceptible to inhibition and activation by a number of substrate analogues. The kinetic and inhibition constants, glycolipid substrate specificity and nucleotide sugar donor specificity have been studied.
Glycolipid glycosyl transferases of a hamster cell line in culture. I. Kinetic constants, substrate and donor nucleotide sugar specificities. The properties of enzymes catalysing the transfer of a galactose from UDP-galactose to exogenous ceramide monohexoside and ceramide di-hexoside derived from the Syrian hamster cell line NIL 2 were studied. The products of these enzymes were characterized by chemical and enzymatic methods. Kinetic analyses showed that the enzymes are susceptible to inhibition and activation by a number of substrate analogues. The kinetic and inhibition constants, glycolipid substrate specificity and nucleotide sugar donor specificity have been studied.