Abstract
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.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
