By Marcel Florkin; Elmer Henry Stotz
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Extra info for Lipid metabolism
In the lactating m a m m a r y gland a galactosyltransferase catalyzes the reaction . 83 S5 87 88 89 90 81 UDP-galactose + iV-acetylglucosamine ^ JV-acetyllactosamine -f U D P The transferase was designated as the A protein. The B protein is a-lactalbumin. A and B proteins combined catalyze the final step in the biosynthesis oflactose. UDP-galactose + glucose ^ lactose + U D P Thus, a-lactalbumin, the B protein, forms a complex with the A protein and thereby changes the acceptor specificity of the A protein.
6 of both the / and D forms was of the competitive type causing large (10-30 fold) increases in the K values of the substrate (UDP-a-D-glucose). Glucose-6-P counteracts the inhibition. These results suggest that not only the D form but also the so-called independent form / of the glycogen synthetase can become com pletely dependent on glucose-6-P for activity. Although b o t h enzymatic activities ( / and D) respond in a qualitatively similar fashion with respect t o inhibition and reactivation there are nevertheless important quantitative differences between / and D forms.
58). There is good evidence that the accumulation of glycogen in the fetus depends u p o n fetal adrenal gland secretions under the influence of the p i t u i t a r y . The rise of glucosyltransferase activity in the fetal rat liver is dependent u p o n the presence of glucocorticosteroid secretion . Therefore, glucocorticosteroids rather than insulin could be responsible for initiation of de novo synthesis of a-glucan-UDP-D-glucose transglucosylase in the fetal rat. 5 4 55 56 56 57 59 60 (Hi) Hormonal regulation of UDP-a-D-glucose-glycogen~glucosyltransferase activity Transferase a c t i v i t y in liver increases about 40 min after insulin admini stration to rats and reaches a peak after about 6 h.